Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator
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Summary: Iron is an essential element for almost all organisms, although an overload of this element results in toxicity because of the formation of hydroxyl radicals. Consequently, most living entities have developed sophisticated mechanisms to control their intracellular iron concentration. In many bacteria, including the opportunistic pathogen Pseudomonas aeruginosa , this task is performed by the ferric uptake regulator (Fur). Fur controls a wide variety of basic physiological processes including iron uptake systems and the expression of exotoxin A. Here, we present the first crystal structure of Fur from P. aeruginosa in complex with Zn 2+ determined at a resolution of 1.8 Å. Furthermore, X‐ray absorption spectroscopic measurements and microPIXE analysis were performed in order to characterize the distinct zinc and iron binding sites in solution. The combination of these complementary techniques enables us to present a model for the activation and DNA binding of the Fur protein.
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Zinc ions were used in all previous Fur structures.
“Zinc ions were used in all previous Fur structures 7 , 14 , 15 , 16 , 17 .”
From Mechanistic insights into metal ion activation and operator recognition by the ferric uptake regulator (2015) · cites this paper as [7]
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984 · see citing works
Raster3D Version 2.0. A program for photorealistic molecular graphics
Merritt, E. A., & Murphy, M. E. P. (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994006396 · Cited by 2,531 · see citing works
Automated protein model building combined with iterative structure refinement.
Perrakis, A., Morris, R. J., & Lamzin, V. S. (1999) · Nature Structural Biology · doi:10.1038/8263 · Cited by 2,423 · see citing works
Fortelle, E. D. L., & Bricogne, G. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)76073-7 · Cited by 1,893 · see citing works
An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
Esnouf, R. M. (1997) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(97)00021-1 · Cited by 1,710 · see citing works
Siderophores: Structure and Function of Microbial Iron Transport Compounds
Neilands, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26723 · Cited by 1,652 · see citing works
Iron Metabolism in Pathogenic Bacteria
Ratledge, C., & Dover, L. G. (2000) · Annual Review of Microbiology · doi:10.1146/annurev.micro.54.1.881 · Cited by 1,539 · see citing works
Main-chain Bond Lengths and Bond Angles in Protein Structures
Laskowski, R. A., Moss, D. S., & Thornton, J. M. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1351 · Cited by 1,217 · see citing works
Liu, W., & Thorp, H. H. (1993) · Inorganic Chemistry · doi:10.1021/ic00071a023 · Cited by 792 · see citing works
Iron and metal regulation in bacteria
Hantke, K. (2001) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(00)00184-3 · Cited by 755 · see citing works
Role of iron in regulation of virulence genes
Litwin, C. M., & Calderwood, S. B. (1993) · Clinical Microbiology Reviews · doi:10.1128/cmr.6.2.137 · Cited by 651 · see citing works
The ZnuABC high‐affinity zinc uptake system and its regulator Zur in <i>Escherichia coli</i>
Patzer, S. I., & Hantke, K. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00883.x · Cited by 490 · see citing works
Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes
Thorp, H. H. (1992) · Inorganic Chemistry · doi:10.1021/ic00035a012 · Cited by 424 · see citing works
Bacterial solutions to the iron-supply problem
Braun, V., & Killmann, H. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01359-6 · Cited by 407 · see citing works
OxyR and SoxRS Regulation of fur
Zheng, M., Doan, B., Schneider, T. D., & Storz, G. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.15.4639-4643.1999 · Cited by 402 · see citing works
Bsat, N., Herbig, A. F., Casillas-Martínez, L., Setlow, P., & Helmann, J. D. (1998) · Molecular Microbiology · doi:10.1046/j.1365-2958.1998.00921.x · Cited by 386 · see citing works
The response of Pseudomonas aeruginosa to iron: genetics, biochemistry and virulence
Vasil, M. L., & Ochsner, U. A. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01586.x · Cited by 367 · see citing works
Self-citationAkerley, B. J., Rubin, E. J., Novick, V. L., Amaya, K. R., Judson, N., & Mekalanos, J. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.012602299 · Cited by 358 · see citing works
Geometry of metal–ligand interactions in proteins
Harding, M. M. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444900019168 · Cited by 348 · see citing works
Miscellaneous Algorithms for Density Modification
Cowtan, K. D., & Main, P. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444997011980 · Cited by 283 · see citing works
Constrained and restrained refinement in EXAFS data analysis with curved wave theory
Binsted, N., Strange, R. W., & Hasnain, S. S. (1992) · Biochemistry · doi:10.1021/bi00163a021 · Cited by 265 · see citing works
Gaballa, A., & Helmann, J. D. (1998) · Journal of Bacteriology · doi:10.1128/jb.180.22.5815-5821.1998 · Cited by 258 · see citing works
Ochsner, U. A., & Vasil, M. L. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4409 · Cited by 254 · see citing works
Self-citationBoyd, J., Oza, M. N., & Murphy, J. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5968 · Cited by 253 · see citing works
Biology and Molecular Epidemiology of Diphtheria Toxin and thetoxGene
Holmes, R. K. (2000) · The Journal of Infectious Diseases · doi:10.1086/315554 · Cited by 233 · see citing works
Patzer, S. I., & Hantke, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m001775200 · Cited by 218 · see citing works
Hall, H. K., & Foster, J. W. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.19.5683-5691.1996 · Cited by 214 · see citing works
Ochsner, U. A., Vasil, A. I., & Vasil, M. L. (1995) · Journal of Bacteriology · doi:10.1128/jb.177.24.7194-7201.1995 · Cited by 198 · see citing works
Self-citationProkaryotic transcription regulators: more than just the helix-turn-helix motif
Huffman, J. L., & Brennan, R. G. (2002) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00295-6 · Cited by 190 · see citing works
Structure of the metal-ion-activated diphtheria toxin repressor/ tox operator complex
White, A., Ding, X., vanderSpek, J. C., Murphy, J. R., & Ringe, D. (1998) · Nature · doi:10.1038/28893 · Cited by 180 · see citing works
Escolar, L., Pérez-Martı́n, J., & de Lorenzo, V. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2119 · Cited by 173 · see citing works
The ferric uptake regulation (Fur) repressor is a zinc metalloprotein
Althaus, E. W., Outten, C. E., Olson, K. E., Cao, H., & O'Halloran, T. V. (1999) · Biochemistry · doi:10.1021/bi982788s · Cited by 147 · see citing works
Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG
Zahrt, T. C., Song, J., Siple, J., & Deretic, V. P. (2001) · Molecular Microbiology · doi:10.1111/j.1365-2958.2001.02321.x · Cited by 136 · see citing works
Pohl, E., Holmes, R. K., & Hol, W. G. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3073 · Cited by 135 · see citing works
Self-citationXiong, A., Singh, V. K., Cabrera, G., & Jayaswal, R. K. (2000) · Microbiology · doi:10.1099/00221287-146-3-659 · Cited by 122 · see citing works
X-ray Absorption Spectroscopy of a New Zinc Site in the Fur Protein fromEscherichia coli
Jacquamet, L., Aberdam, D., Adrait, A., Hazemann, J., Latour, J., & Michaud‐Soret, I. (1998) · Biochemistry · doi:10.1021/bi9721344 · Cited by 119 · see citing works
Pohl, E., Holmes, R. K., & Hol, W. G. J. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2339 · Cited by 117 · see citing works
Self-citationBarton, H. A., Johnson, Z., Cox, C. D., Vasil, A. I., & Vasil, M. L. (1996) · Molecular Microbiology · doi:10.1046/j.1365-2958.1996.381426.x · Cited by 113 · see citing works
Self-citationQiu, X., Verlinde, C. L. M. J., Zhang, S., Schmitt, M. P., Holmes, R. K., & Hol, W. G. J. (1995) · Structure · doi:10.1016/s0969-2126(01)00137-x · Cited by 112 · see citing works
Tao, X., & Murphy, J. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36677-3 · Cited by 95 · see citing works
Pseudomonas aeruginosa fur Overlaps with a Gene Encoding a Novel Outer Membrane Lipoprotein, OmlA
Ochsner, U. A., Vasil, A. I., Johnson, Z., & Vasil, M. L. (1999) · Journal of Bacteriology · doi:10.1128/jb.181.4.1099-1109.1999 · Cited by 94 · see citing works
Self-citationIdentification and cloning of a fur homolog from Neisseria gonorrhoeae
Berish, S. A., Subbarao, S., Chen, C. Y., Trees, D. L., & Morse, S. A. (1993) · Infection and Immunity · doi:10.1128/iai.61.11.4599-4606.1993 · Cited by 92 · see citing works
Schiering, N., Tao, X., Zeng, H., Murphy, J. R., Petsko, G. A., & Ringe, D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.21.9843 · Cited by 92 · see citing works
SHELX Applications to Macromolecules
Sheldrick, G. M. (1998) · Springer eBooks · doi:10.1007/978-94-015-9093-8_35 · Cited by 91 · see citing works
Qiu, X., Pohl, E., Holmes, R. K., & Hol, W. G. J. (1996) · Biochemistry · doi:10.1021/bi960861d · Cited by 89 · see citing works
Self-citationDing, X., Zeng, H., Schiering, N., Ringe, D., & Murphy, J. R. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0496-382 · Cited by 86 · see citing works
Prince, R. W., Storey, D. G., Vasil, A. I., & Vasil, M. L. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb01991.x · Cited by 77 · see citing works
Self-citationFeese, M. D., Ingason, B. P., Goranson-Siekierke, J., Holmes, R. K., & Hol, W. G. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007531200 · Cited by 76 · see citing works
Purification and characterization of the diphtheria toxin repressor.
Schmitt, M. P., Twiddy, E. M., & Holmes, R. K. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7576 · Cited by 74 · see citing works
Pohl, E., Holmes, R. K., & Hol, W. G. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.35.22420 · Cited by 66 · see citing works
Self-citationGonzalez de Peredo, A., Saint-Pierre, C., Adrait, A., Jacquamet, L., Latour, J.-M., Michaud-Soret, I., & Forest, E. (1999) · Biochemistry · doi:10.1021/bi9902283 · Cited by 63 · see citing works
Escolar, L., Pérez‐Martín, J., & de Lorenzo, V. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002839200 · Cited by 56 · see citing works
de Peredo, A. G., Saint‐Pierre, C., Latour, J., Michaud‐Soret, I., & Forest, É. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4769 · Cited by 55 · see citing works
Regulation of mammalian iron homeostasis
Schneider, B. D., & Leibold, E. A. (2000) · Current Opinion in Clinical Nutrition & Metabolic Care · doi:10.1097/00075197-200007000-00005 · Cited by 52 · see citing works
George, G. N., Hedman, B., & Hodgson, K. O. (1998) · Nature Structural Biology · doi:10.1038/1336 · Cited by 40 · see citing works
Leaving no element of doubt: analysis of proteins using microPIXE
Garman, E. F. (1999) · Structure · doi:10.1016/s0969-2126(00)88335-5 · Cited by 40 · see citing works
Self-citationStructures of three diphtheria toxin repressor (DtxR) variants with decreased repressor activity
Pohl, E., Goranson-Siekierke, J., Choi, M. K., Roosild, T. P., Holmes, R. K., & Hol, W. G. J. (2001) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744490100230x · Cited by 14 · see citing works
Self-citation
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Research works printed but not linked: 1
- Barton, H.A. (1997) Structure and functional analysis of Pseudomonas aeruginosa Fur repressor. PhD Thesis, University of Colorado Health Sciences Center.
Cited by
Sorted by citations
Andrews, S. C., Robinson, A. K., & Rodríguez-Quiñones, F. (2003) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(03)00055-x · Cited by 2,702 · see citing works
Siderophore-Based Iron Acquisition and Pathogen Control
Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774 · see citing works
Bacterial Iron Sources: From Siderophores to Hemophores
Wandersman, C., & Delepelaire, P. (2004) · Annual Review of Microbiology · doi:10.1146/annurev.micro.58.030603.123811 · Cited by 1,056 · see citing works
Metal homeostasis and resistance in bacteria
Chandrangsu, P., Rensing, C., & Helmann, J. D. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2017.15 · Cited by 812 · see citing works
Coordination Chemistry of Bacterial Metal Transport and Sensing
Ma, Z., Jacobsen, F. E., & Giedroc, D. P. (2009) · Chemical Reviews · doi:10.1021/cr900077w · Cited by 622 · see citing works
A dynamic and intricate regulatory network determines Pseudomonas aeruginosa virulence
Balasubramanian, D., Schneper, L. M., Kumari, H., & Mathee, K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1039 · Cited by 590 · see citing works
The PerR transcription factor senses H2O2 by metal-catalysed histidine oxidation
Lee, J.-W., & Helmann, J. D. (2006) · Nature · doi:10.1038/nature04537 · Cited by 547 · see citing works
Microbial Iron Acquisition: Marine and Terrestrial Siderophores
Sandy, M., & Butler, A. (2009) · Chemical Reviews · doi:10.1021/cr9002787 · Cited by 490 · see citing works
Wilderman, P. J., Sowa, N. A., FitzGerald, D. J., FitzGerald, P. C., Gottesman, S., Ochsner, U. A., & Vasil, M. L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403423101 · Cited by 455 · see citing works
Self-citationFunctional specialization within the Fur family of metalloregulators
Lee, J.-W., & Helmann, J. D. (2007) · BioMetals · doi:10.1007/s10534-006-9070-7 · Cited by 432 · see citing works
At the Crossroads of Bacterial Metabolism and Virulence Factor Synthesis in Staphylococci
Somerville, G. A., & Proctor, R. A. (2009) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00005-09 · Cited by 391 · see citing works
Fillat, M. F. (2014) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2014.01.029 · Cited by 329 · see citing works
Lehnert, N., Kim, E., Dong, H. T., Harland, J. B., Hunt, A. P., Manickas, E. C., Oakley, K. M., Pham, J., Reed, G. C., & Alfaro, V. S. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.1c00253 · Cited by 277 · see citing works
Grass, G., Otto, M., Fricke, B., Haney, C. J., Rensing, C., Nies, D. H., & Munkelt, D. (2005) · Archives of Microbiology · doi:10.1007/s00203-004-0739-4 · Cited by 233 · see citing works
Bolaños-García, V. M., & Davies, O. R. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2006.03.027 · Cited by 232 · see citing works
This Is Not Your Mother's Repressor: the Complex Role of Fur in Pathogenesis
Carpenter, B. M., Whitmire, J. M., & Merrell, D. S. (2009) · Infection and Immunity · doi:10.1128/iai.00116-09 · Cited by 215 · see citing works
Nickel Homeostasis and Nickel Regulation: An Overview
Li, Y., & Zamble, D. B. (2009) · Chemical Reviews · doi:10.1021/cr900010n · Cited by 217 · see citing works
Metal sensor proteins: nature's metalloregulated allosteric switches
Giedroc, D. P., & Arunkumar, A. I. (2007) · Dalton Transactions · doi:10.1039/b706769k · Cited by 213 · see citing works
Metal ion homeostasis in Bacillus subtilis
Moore, C. M., & Helmann, J. D. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.02.007 · Cited by 204 · see citing works
Iron and heme utilization inPorphyromonas gingivalis
Olczak, T., Simpson, W., Liu, X., & Genco, C. A. (2004) · FEMS Microbiology Reviews · doi:10.1016/j.femsre.2004.09.001 · Cited by 199 · see citing works
Sheldon, J. R., & Skaar, E. P. (2020) · PLOS Pathogens · doi:10.1371/journal.ppat.1008995 · Cited by 177 · see citing works
Metalloregulatory proteins: Metal selectivity and allosteric switching
Reyes-Caballero, H., Campanello, G. C., & Giedroc, D. P. (2011) · Biophysical Chemistry · doi:10.1016/j.bpc.2011.03.010 · Cited by 169 · see citing works
Metalloproteomics, metalloproteomes, and the annotation of metalloproteins
Maret, W. (2010) · Metallomics · doi:10.1039/b915804a · Cited by 172 · see citing works
Rodionov, D. A., Gelfand, M. S., Todd, J. D., Curson, A. R. J., & Johnston, A. W. B. (2005) · PLoS Computational Biology · doi:10.1371/journal.pcbi.0020163 · Cited by 147 · see citing works
Bacterial iron detoxification at the molecular level
Bradley, J. M., Svistunenko, D. A., Wilson, M. T., Hemmings, A. M., Moore, G. R., & Le Brun, N. E. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.007746 · Cited by 140 · see citing works
Crystal Structure and Function of the Zinc Uptake Regulator FurB from Mycobacterium tuberculosis
Lucarelli, D., Russo, S., Garman, E. F., Milano, A., Meyer‐Klaucke, W., & Pohl, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609974200 · Cited by 144 · see citing works
Self-citationAhn, B., Cha, J., Lee, E., Han, A. R., Thompson, C. J., & Roe, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05065.x · Cited by 145 · see citing works
Pennella, M. A., & Giedroc, D. P. (2005) · BioMetals · doi:10.1007/s10534-005-3716-8 · Cited by 142 · see citing works
Butcher, J., Sarvan, S., Brunzelle, J. S., Couture, J.-F., & Stintzi, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1118321109 · Cited by 137 · see citing works
Wan, X., VerBerkmoes, N. C., McCue, L. A., Stanek, D., Connelly, H. M., Hauser, L., Wu, L., Liu, X., Yan, T., Leaphart, A. B., et al. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.24.8385-8400.2004 · Cited by 132 · see citing works
Dian, C., Vitale, S., Leonard, G. A., Bahlawane, C., Fauquant, C., Leduc, D., Muller, C., Reuse, H. D., Michaud‐Soret, I., & Terradot, L. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07517.x · Cited by 127 · see citing works
Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur
Shin, J.-H., Jung, H. J., An, Y. J., Cho, Y.-B., Cha, S.-S., & Roe, J.-H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017744108 · Cited by 124 · see citing works
Sheikh, M. A., & Taylor, G. L. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06718.x · Cited by 126 · see citing works
Lee, J., & Helmann, J. D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603968200 · Cited by 124 · see citing works
Bacterial metal-sensing proteins exemplified by ArsR–SmtB family repressors
Osman, D., & Cavet, J. S. (2010) · Natural Product Reports · doi:10.1039/b906682a · Cited by 124 · see citing works
Miethke, M. (2012) · Metallomics · doi:10.1039/c2mt20193c · Cited by 121 · see citing works
Shin, J., Oh, S., Kim, S., & Roe, J. (2007) · Journal of Bacteriology · doi:10.1128/jb.01851-06 · Cited by 118 · see citing works
Recognition of DNA by Three Ferric Uptake Regulator (Fur) Homologs inBacillus subtilis
Fuangthong, M., & Helmann, J. D. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.21.6348-6357.2003 · Cited by 117 · see citing works
Deng, Z., Wang, Q., Liu, Z., Zhang, M., Machado, A. C. D., Chiu, T.-P., Feng, C., Zhang, Q., Yu, L., Qi, L., et al. (2015) · Nature Communications · doi:10.1038/ncomms8642 · Cited by 117 · see citing works
Structural and Mechanistic Basis of Zinc Regulation Across the E. coli Zur Regulon
Gilston, B. A., Wang, S., Marcus, M. D., Canalizo-Hernández, M. A., Swindell, E. P., Xue, Y., Mondragón, A., & O’Halloran, T. V. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001987 · Cited by 115 · see citing works
Pecqueur, L., D'Autréaux, B., Dupuy, J., Nicolet, Y., Jacquamet, L., Brutscher, B., Michaud-Soret, I., & Bersch, B. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601278200 · Cited by 116 · see citing works
Bacterial zinc uptake regulator proteins and their regulons
Mikhaylina, A., Ksibe, A. Z., Scanlan, D. J., & Blindauer, C. A. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170228 · Cited by 114 · see citing works
Jacquamet, L., Traoré, D. A. K., Ferrer, J.-L., Proux, O., Testemale, D., Hazemann, J., Nazarenko, E. S., Ghazouani, A. E., Caux‐Thang, C., Duarte, V., et al. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06753.x · Cited by 113 · see citing works
The Fur-like protein Mur of Rhizobium leguminosarum is a Mn2+-responsive transcriptional regulator
Díaz-Mireles, E., Wexler, M., Sawers, R. G., Bellini, D., Todd, J. D., & Johnston, A. W. B. (2004) · Microbiology · doi:10.1099/mic.0.26961-0 · Cited by 111 · see citing works
van Rij, T., Girard, G., Lugtenberg, B. J. J., & Bloemberg, G. V. (2005) · Microbiology · doi:10.1099/mic.0.28063-0 · Cited by 108 · see citing works
How we learnt about iron acquisition in Pseudomonas aeruginosa: a series of very fortunate events
Vasil, M. L. (2006) · BioMetals · doi:10.1007/s10534-006-9067-2 · Cited by 107 · see citing works
Self-citationCrystal structure of the apo‐PerR‐Zn protein from Bacillus subtilis
Traoré, D. A. K., Ghazouani, A. E., Ilango, S., Dupuy, J., Jacquamet, L., Ferrer, J.-L., Caux‐Thang, C., Duarte, V., & Latour, J. (2006) · Molecular Microbiology · doi:10.1111/j.1365-2958.2006.05313.x · Cited by 107 · see citing works
Iron-containing transcription factors and their roles as sensors
Fleischhacker, A. S., & Kiley, P. J. (2011) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2011.01.006 · Cited by 105 · see citing works
Sequential binding and sensing of Zn(II) by Bacillus subtilis Zur
Ma, Z., Gabriel, S. E., & Helmann, J. D. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr625 · Cited by 98 · see citing works
D’Autréaux, B., Horner, O., Oddou, J., Jeandey, C., Gambarelli, S., Berthomieu, C., Latour, J., & Michaud‐Soret, I. (2004) · Journal of the American Chemical Society · doi:10.1021/ja031671a · Cited by 96 · see citing works
Structure of the manganese-bound manganese transport regulator of Bacillus subtilis
Glasfeld, A., Guédon, E., Helmann, J. D., & Brennan, R. G. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb951 · Cited by 93 · see citing works
Elemental analysis of proteins by microPIXE
Garman, E. F., & Grime, G. W. (2004) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2004.09.005 · Cited by 91 · see citing works
Self-citationDiscovery of Fur binding site clusters in Escherichia coli by information theory models
Chen, Z., Lewis, K. A., Shultzaberger, R. K., Lyakhov, I. G., Zheng, M., Doan, B., Storz, G., & Schneider, T. D. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm631 · Cited by 88 · see citing works
Beyond the Fur paradigm: iron-controlled gene expression in rhizobia
Rudolph, G., Hennecke, H., & Fischer, H. (2006) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2006.00030.x · Cited by 88 · see citing works
Regulation of Sialic Acid Catabolism by the DNA Binding Protein NanR in Escherichia coli
Kalivoda, K. A., Steenbergen, S. M., Vimr, E. R., & PLUMBRIDGE, J. A. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.16.4806-4815.2003 · Cited by 86 · see citing works
Agnoli, K., Lowe, C. A., Farmer, K. L., Husnain, S. I., & Thomas, M. S. (2006) · Journal of Bacteriology · doi:10.1128/jb.188.10.3631-3644.2006 · Cited by 86 · see citing works
Kranzler, C. F., Rudolf, M., Keren, N., & Schleiff, E. (2012) · Advances in botanical research · doi:10.1016/b978-0-12-394313-2.00003-2 · Cited by 85 · see citing works
Comparative and Functional Genomic Analyses of Iron Transport and Regulation in Leptospira spp
Louvel, H., Bommezzadri, S., Zidane, N., Boursaux‐Eude, C., Créno, S., Magnier, A., Rouy, Z., Médigue, C., Girons, I. S., Bouchier, C., et al. (2006) · Journal of Bacteriology · doi:10.1128/jb.00711-06 · Cited by 80 · see citing works
Metal site occupancy and allosteric switching in bacterial metal sensor proteins
Guerra, A. J., & Giedroc, D. P. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.11.021 · Cited by 77 · see citing works
Emerging patterns of plasmid-host coevolution that stabilize antibiotic resistance
Stalder, T., Rogers, L. M., Renfrow, C., Yano, H., Smith, Z., & Top, E. M. (2017) · Scientific Reports · doi:10.1038/s41598-017-04662-0 · Cited by 77 · see citing works
Kunkle, C. A., & Schmitt, M. P. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.23.6826-6840.2003 · Cited by 71 · see citing works
Kliegman, J. I., Griner, S. L., Helmann, J. D., Brennan, R. G., & Glasfeld, A. (2006) · Biochemistry · doi:10.1021/bi0524215 · Cited by 73 · see citing works
Koch, D., Nies, D. H., & Grass, G. (2006) · BioMetals · doi:10.1007/s10534-006-9039-6 · Cited by 73 · see citing works
Global analysis of iron assimilation and fur regulation in Yersinia pestis
Zhou, D., Qin, L., Han, Y., Qiu, J., Chen, Z., Li, B., Song, Y., Wang, J., Guo, Z., Zhai, J., et al. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00208.x · Cited by 72 · see citing works
Uebe, R., Voigt, B., Schweder, T., Albrecht, D., Katzmann, E., Lang, C., Böttger, L. H., Matzanke, B. F., & Schüler, D. (2010) · Journal of Bacteriology · doi:10.1128/jb.00319-10 · Cited by 69 · see citing works
Bacillus cereus Fur regulates iron metabolism and is required for full virulence
Harvie, D. R., Vı́lchez, S., Steggles, J. R., & Ellar, D. J. (2005) · Microbiology · doi:10.1099/mic.0.27744-0 · Cited by 70 · see citing works
Feng, Y., Li, M., Zhang, H., Zheng, B., Han, H., Wang, C., Yan, J., Tang, J., & Gao, G. F. (2008) · Journal of Bacteriology · doi:10.1128/jb.01532-07 · Cited by 68 · see citing works
Hibbing, M. E., & Fuqua, C. (2011) · Journal of Bacteriology · doi:10.1128/jb.00317-11 · Cited by 67 · see citing works
Santander, J., Golden, G., Wanda, S.-Y., & Curtiss, R. (2012) · Infection and Immunity · doi:10.1128/iai.00013-12 · Cited by 67 · see citing works
An, Y. J., Ahn, B., Han, A.-R., Kim, H.-M., Chung, K. M., Shin, J., Cho, Y., Roe, J., & Cha, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp198 · Cited by 66 · see citing works
Pennella, M. A., Arunkumar, A. I., & Giedroc, D. P. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.12.019 · Cited by 65 · see citing works
Liu, T., Nakashima, S., Hirose, K., Shibasaka, M., Katsuhara, M., Ezaki, B., Giedroc, D. P., & Kasamo, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310560200 · Cited by 64 · see citing works
Ma, Z., Faulkner, M. J., & Helmann, J. D. (2012) · Molecular Microbiology · doi:10.1111/mmi.12049 · Cited by 62 · see citing works
Danielli, A., & Scarlato, V. (2010) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2010.00233.x · Cited by 62 · see citing works
Advanced nuclear analytical techniques for metalloproteomics
Gao, Y., Chen, C., & Chai, Z. (2007) · Journal of Analytical Atomic Spectrometry · doi:10.1039/b703323k · Cited by 62 · see citing works
Locatelli, F. M., Goo, K.-S., & Ulanová, D. (2016) · Metallomics · doi:10.1039/c5mt00324e · Cited by 61 · see citing works
Mining Genomes of Marine Cyanobacteria for Elements of Zinc Homeostasis
Barnett, J. P., Millard, A. D., Ksibe, A. Z., Scanlan, D. J., Schmid, R., & Blindauer, C. A. (2012) · Frontiers in Microbiology · doi:10.3389/fmicb.2012.00142 · Cited by 59 · see citing works
Seshu, J., Boylan, J. A., Hyde, J. A., Swingle, K., Gherardini, F. C., & Skare, J. T. (2004) · Molecular Microbiology · doi:10.1111/j.1365-2958.2004.04352.x · Cited by 59 · see citing works
Platero, R., Peixoto, L., O’Brian, M. R., & Fabiano, E. (2004) · Applied and Environmental Microbiology · doi:10.1128/aem.70.7.4349-4355.2004 · Cited by 59 · see citing works
The Fur Homologue inBorrelia burgdorferi
Katona, L. I., Tokarz, R., Kuhlow, C. J., Benach, J., & Benach, J. L. (2004) · Journal of Bacteriology · doi:10.1128/jb.186.19.6443-6456.2004 · Cited by 58 · see citing works
Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking
Capdevila, D. A., Rondón, J. J., Edmonds, K. A., Rocchio, J. S., Dujovne, M. V., & Giedroc, D. P. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00264 · Cited by 59 · see citing works
López-Gomollón, S., Sevilla, E., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2008) · Biochemical Journal · doi:10.1042/bj20081066 · Cited by 56 · see citing works
Qiu, X., Han, S., Hu, Y., Gao, M., & Wang, H. (2013) · Journal of Materials Chemistry A · doi:10.1039/c3ta14314g · Cited by 56 · see citing works
Characterization of the Fur Regulon in Pseudomonas syringae pv. tomato DC3000
Butcher, B. G., Bronstein, P. A., Myers, C. R., Stodghill, P. V., Bolton, J. J., Markel, E. J., Filiatrault, M. J., Swingle, B. M., Gaballa, A., Helmann, J. D., et al. (2011) · Journal of Bacteriology · doi:10.1128/jb.00340-11 · Cited by 55 · see citing works
Yeoman, K. H. (2004) · Microbiology · doi:10.1099/mic.0.27419-0 · Cited by 54 · see citing works
Structural insights into protein–metal ion partnerships
Barondeau, D. P., & Getzoff, E. D. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.10.012 · Cited by 54 · see citing works
Small, S. K., Puri, S., & O’Brian, M. R. (2008) · BioMetals · doi:10.1007/s10534-008-9192-1 · Cited by 53 · see citing works
Three fur homologues from Anabaena sp. PCC7120: exploring reciprocal protein-promoter recognition
Hernández, J. L., López-Gomollón, S., Bes, M. T., Fillat, M. F., & Peleato, M. L. (2004) · FEMS Microbiology Letters · doi:10.1016/j.femsle.2004.05.050 · Cited by 58 · see citing works
Fur-Mediated Global Regulatory Circuits in Pathogenic Neisseria Species
Yu, C., & Genco, C. A. (2012) · Journal of Bacteriology · doi:10.1128/jb.00262-12 · Cited by 51 · see citing works
Hernández‐Rivas, J., López-Gomollón, S., Muro-Pastor, A. M., Valladares, A., Bes, M. T., Peleato, M. L., & Fillat, M. F. (2006) · BioMetals · doi:10.1007/s10534-005-7750-3 · Cited by 52 · see citing works
Zhang, F., Li, B., Dong, H., Chen, M., Yao, S., Li, J., Zhang, H., Liu, X., Wang, H., Song, N., et al. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa696 · Cited by 49 · see citing works
“According to crystal structure of Fur in Pseudomonas aeruginosa and Vibrio cholera , each monomer of the dimeric Fur protein has two metal-binding sites––one is responsible for regulation and the other for structural stabilization (63,64).”
Ando, H., Kitao, T., Miyoshi‐Akiyama, T., Kato, S., Mori, T., & Kirikae, T. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07547.x · Cited by 55 · see citing works
Adhikary, S., Saha, J., Dutta, P., & Pal, A. (2024) · Geomicrobiology Journal · doi:10.1080/01490451.2024.2340517 · Cited by 50 · see citing works
Three fur homologues from Anabaena sp. PCC7120: exploring reciprocal protein-promoter recognition
Hernández, J. A., López-Gomollón, S., Bes, M. T., Fillat, M. F., & Peleato, M. L. (2004) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2004.tb09658.x · Cited by 51 · see citing works
Limited Role for Iron Regulation in <i>Coxiella burnetii</i> Pathogenesis
Briggs, H. L., Pul, N., Seshadri, R., Wilson, M. J., Tersteeg, C., Russell-Lodrigue, K. E., Andoh, M., Bäumler, A. J., & Samuel, J. E. (2008) · Infection and Immunity · doi:10.1128/iai.01609-07 · Cited by 52 · see citing works
Dimeric Brucella abortus Irr protein controls its own expression and binds haem
Martínez, M., Ugalde, R. A., & Almirón, M. A. (2005) · Microbiology · doi:10.1099/mic.0.28213-0 · Cited by 49 · see citing works
Iron acquisition and regulation systems in Streptococcus species
Ge, R., & Sun, X. (2014) · Metallomics · doi:10.1039/c4mt00011k · Cited by 48 · see citing works
Cha, J. Y., Lee, J. S., Oh, J., Choi, J. W., & Baik, H. S. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.11.021 · Cited by 48 · see citing works
Structure and Function of an ADP-Ribose-Dependent Transcriptional Regulator of NAD Metabolism
Huang, N. N., Ingeniis, J. D., Galeazzi, L., Mancini, C., Korostelev, Y., Rakhmaninova, A. B., Gelfand, M. S., Rodionov, D. A., Raffaelli, N., & Zhang, H. (2009) · Structure · doi:10.1016/j.str.2009.05.012 · Cited by 48 · see citing works
Pich, Ò. Q., Carpenter, B. M., Gilbreath, J. J., & Merrell, D. S. (2012) · Molecular Microbiology · doi:10.1111/j.1365-2958.2012.08066.x · Cited by 47 · see citing works
- Authors
- Pohl, E., Haller, J. C., Mijovilovich, A., Meyer‐Klaucke, W., Garman, E., & Vasil, M. L.
- Affiliations
- European Molecular Biology Laboratory (DE)
- University of Oxford (GB)
- Corresponding author
- Pohl, Ehmke
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-02
- Volume
- 47
- Issue
- 4
- Pages
- 903-915
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2098798603
- Cited by
- 326
- References
- 62
- Citations by year
- 2026: 4 · 2025: 6 · 2024: 8 · 2023: 8 · 2022: 8 · 2021: 6 · 2020: 11 · 2019: 13 · 2018: 9 · 2017: 16 · 2016: 10 · 2015: 10 · 2014: 20 · 2013: 14 · 2012: 23
- FWCI
- 15.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- Durham Research Online (Durham University) (acceptedVersion)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion)
- Durham Research Online (Durham University) (submittedVersion, cc-by)
- Funders
- National Institutes of Health
- National Institute of Allergy and Infectious Diseases (AI-15490)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- ferric uptake regulator, Fur protein, Pseudomonas aeruginosa, iron homeostasis, zinc binding, iron binding, protein crystal structure, DNA binding, transcriptional regulation, exotoxin A, X-ray absorption spectroscopy
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, DNA, Bacterial, Homeostasis, Iron, Models, Molecular, Molecular Sequence Data, Protein Conformation, Pseudomonas aeruginosa, Repressor Proteins, Spectrometry, X-Ray Emission, Spectrum Analysis, X-Rays, Molecular Structure, Sequence Homology, Amino Acid, Crystallography, X-Ray, Macromolecular Substances, Static Electricity
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