The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
Open accessAbstract
HAMP domains connect extracellular sensory with intracellular signaling domains in over 7500 proteins, including histidine kinases, adenylyl cyclases, chemotaxis receptors, and phosphatases. The solution structure of an archaeal HAMP domain shows a homodimeric, four-helical, parallel coiled coil with unusual interhelical packing, related to the canonical packing by rotation of the helices. This suggests a model for the mechanism of signal transduction, in which HAMP alternates between the observed conformation and a canonical coiled coil. We explored this mechanism in vitro and in vivo using HAMP domain fusions with a mycobacterial adenylyl cyclase and an E. coli chemotaxis receptor. Structural and functional studies show that the equilibrium between the two forms is dependent on the side-chain size of residue 291, which is alanine in the wild-type protein.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Natural coiled coils are dynamic and play central roles in a multitude of biological functions.
“Natural coiled coils, on the other hand, are dynamic and play central roles in a multitude of biological functions.13−17”
From Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints (2025) · cites this paper as [13]
Cites
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
Altschul, S. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.17.3389 · Cited by 73,302 · see citing works
Thompson, J. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.24.4876 · Cited by 39,119 · see citing works
PROCHECK: a program to check the stereochemical quality of protein structures
Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,694 · see citing works
Protein backbone angle restraints from searching a database for chemical shift and sequence homology
Cornilescu, G., Delaglio, F., & Bax, A. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008392405740 · Cited by 2,957 · see citing works
Berg, H. C. (1984) · Princeton University Press eBooks · doi:10.1515/9780691279886 · Cited by 2,400 · see citing works
The Xplor-NIH NMR molecular structure determination package
Schwieters, C. D., Kuszewski, J. J., Tjandra, N., & Clore, G. M. (2003) · Journal of Magnetic Resonance · doi:10.1016/s1090-7807(02)00014-9 · Cited by 2,371 · see citing works
Farrow, N. A., Muhandiram, R., Singer, A. U., Pascal, S. M., Kay, C. M., Gish, G., Shoelson, S. E., Pawson, T. J., Forman-Kay, J. D., & Kay, L. E. (1994) · Biochemistry · doi:10.1021/bi00185a040 · Cited by 2,094 · see citing works
The packing of α-helices: simple coiled-coils
Crick, F. H. C. (1953) · Acta Crystallographica · doi:10.1107/s0365110x53001964 · Cited by 1,578 · see citing works
The Structure of α-Helical Coiled Coils
Lupas, A. N., & Gruber, M. (2005) · Advances in protein chemistry · doi:10.1016/s0065-3233(05)70003-6 · Cited by 668 · see citing works
Self-citationFour-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor
Kim, K. K., Yokota, H. A., & Kim, S. (1999) · Nature · doi:10.1038/23512 · Cited by 445 · see citing works
Aravind, L., & Ponting, C. P. (1999) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1999.tb13650.x · Cited by 411 · see citing works
Evolution of Two-Component Signal Transduction
Koretke, K. K., Lupas, A. N., Warren, P. V., Rosenberg, M. J., & Brown, J. R. (2000) · Molecular Biology and Evolution · doi:10.1093/oxfordjournals.molbev.a026297 · Cited by 315 · see citing works
Self-citationA Piston Model for Transmembrane Signaling of the Aspartate Receptor
Ottemann, K. M., Xiao, W., Shin, Y., & Koshland, D. E. (1999) · Science · doi:10.1126/science.285.5434.1751 · Cited by 270 · see citing works
Molecular mechanism of transmembrane signaling by the aspartate receptor: a model.
Chervitz, S. A., & Falke, J. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.6.2545 · Cited by 238 · see citing works
Utsumi, R., Brissette, R. E., Rampersaud, A., Forst, S., Oosawa, K., & Inouye, M. (1989) · Science · doi:10.1126/science.2476847 · Cited by 210 · see citing works
Development of the signal in sensory rhodopsin and its transfer to the cognate transducer
Moukhametzianov, R., Klare, J. P., Efremov, R. G., Baeken, C., Göppner, A., Labahn, J., Engelhard, M., Büldt, G., & Gordeliy, V. (2006) · Nature · doi:10.1038/nature04520 · Cited by 185 · see citing works
Histidine Kinases in Signal Transduction
(2003) · Elsevier eBooks · doi:10.1016/b978-0-12-372484-7.x5000-0 · Cited by 148 · see citing works
Williams, S. B., & Stewart, V. J. (1999) · Molecular Microbiology · doi:10.1046/j.1365-2958.1999.01562.x · Cited by 141 · see citing works
Historical review: Another 50th anniversary – new periodicities in coiled coils
Gruber, M. (2003) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.10.008 · Cited by 141 · see citing works
Self-citationThe Structure of a pH-Sensing Mycobacterial Adenylyl Cyclase Holoenzyme
Tews, I., Findeisen, F., Sinning, I., Schultz, A. C. F., Schultz, J. E., & Linder, J. U. (2005) · Science · doi:10.1126/science.1107642 · Cited by 132 · see citing works
Self-citationMeasurement of fast proton exchange rates in isotopically labeled compounds
Gemmecker, G., Jahnke, W., & Kessler, H. (1993) · Journal of the American Chemical Society · doi:10.1021/ja00077a080 · Cited by 130 · see citing works
Butler, S. L., & Falke, J. J. (1998) · Biochemistry · doi:10.1021/bi980607g · Cited by 115 · see citing works
The Alacoil: A very tight, antiparallel coiled‐coil of helices
Gernert, K. M., Surles, M. C., LaBean, T. H., Richardson, J. S., & Richardson, D. C. (1995) · Protein Science · doi:10.1002/pro.5560041102 · Cited by 111 · see citing works
Cochran, A. G., & Kim, P. S. (1996) · Science · doi:10.1126/science.271.5252.1113 · Cited by 100 · see citing works
Genetic analysis of the leucine heptad repeats of Lac repressor: evidence for a 4‐helical bundle.
Alberti, S., Oehler, S., von Wilcken‐Bergmann, B., & Müller‐Hill, B. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05992.x · Cited by 88 · see citing works
Appleman, J. A., & Stewart, V. J. (2002) · Journal of Bacteriology · doi:10.1128/jb.185.1.89-97.2003 · Cited by 88 · see citing works
Appleman, J. A., Chen, L., & Stewart, V. J. (2003) · Journal of Bacteriology · doi:10.1128/jb.185.16.4872-4882.2003 · Cited by 84 · see citing works
Side Chains at the Membrane−Water Interface Modulate the Signaling State of a Transmembrane Receptor
Miller, A. S., & Falke, J. J. (2004) · Biochemistry · doi:10.1021/bi0360206 · Cited by 84 · see citing works
An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments
Diercks, T., Coles, M. P., & Kessler, H. (1999) · Journal of Biomolecular NMR · doi:10.1023/a:1008367912535 · Cited by 80 · see citing works
Self-citationWang, A. C., & Bax, A. (1995) · Journal of the American Chemical Society · doi:10.1021/ja00111a021 · Cited by 80 · see citing works
Computational learning reveals coiled coil-like motifs in histidine kinase linker domains
Singh, M., Berger, B., Kim, P. S., Berger, J. M., & Cochran, A. G. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.6.2738 · Cited by 80 · see citing works
Origin of asymmetry in adenylyl cyclases: structures of Mycobacterium tuberculosis Rv1900c
Sinha, S. C., Wetterer, M., Sprang, S. R., Schultz, J. E., & Linder, J. U. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600573 · Cited by 78 · see citing works
Self-citationStructural Analysis of a HAMP Domain
Bordignon, E., Klare, J. P., Doebber, M., Wegener, A. A., Martell, S., Engelhard, M., & Steinhoff, H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509391200 · Cited by 75 · see citing works
Yadav, M. K., Leman, L. J., Price, D. J., Brooks, C. L., Stout, C. D., & Ghadiri, M. R. (2006) · Biochemistry · doi:10.1021/bi060092q · Cited by 74 · see citing works
The solution structure of the N-terminal domain of riboflavin synthase
Truffault, V., Coles, M. P., Diercks, T., Abelmann, K., Eberhardt, S., Lüttgen, H., Bacher, A., & Kessler, H. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4683 · Cited by 66 · see citing works
Self-citationAntiparallel Four-Stranded Coiled Coil Specified by a 3-3-1 Hydrophobic Heptad Repeat
Deng, Y., Liu, J., Zheng, Q., Eliezer, D., Kallenbach, N. R., & Lu, M. (2006) · Structure · doi:10.1016/j.str.2005.10.010 · Cited by 59 · see citing works
Tokishita, S., Kojima, A., & Mizuno, T. (1992) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a123823 · Cited by 56 · see citing works
Tao, W., Malone, C. L., Ault, A. D., Deschenes, R. J., & Fassler, J. S. (2002) · Molecular Microbiology · doi:10.1046/j.1365-2958.2002.02757.x · Cited by 56 · see citing works
Zhu, Y., & Inouye, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300916200 · Cited by 49 · see citing works
Measurement of intrinsic exchange rates of amide protons in a 15N-labeled peptide
Koide, S., Jahnke, W., & Wright, P. E. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197811 · Cited by 46 · see citing works
The effect of HAMP domains on class IIIb adenylyl cyclases from Mycobacterium tuberculosis
Linder, J. U., Hammer, A., & Schultz, J. E. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04172.x · Cited by 45 · see citing works
Self-citationStructure-Based Engineering of Internal Cavities in Coiled-Coil Peptides,
Yadav, M. K., Redman, J. E., Leman, L. J., Alvarez-Gutierrez, J. M., Zhang, Y., Stout, C. D., & Ghadiri, M. R. (2005) · Biochemistry · doi:10.1021/bi050742a · Cited by 38 · see citing works
Jin, T., & Inouye, M. (1994) · Journal of Molecular Biology · doi:10.1006/jmbi.1994.1746 · Cited by 35 · see citing works
Transmembrane signalling and the aspartate receptor
Scott, W. G., & Stoddard, B. L. (1994) · Structure · doi:10.1016/s0969-2126(94)00088-3 · Cited by 30 · see citing works
Solan, A. K., Ratia, K. M., & Fairman, R. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2002.5427 · Cited by 14 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Biological Insights from Structures of Two-Component Proteins
Gao, R., & Stock, A. (2009) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073214 · Cited by 793 · see citing works
Bacterial chemoreceptors: high-performance signaling in networked arrays
Hazelbauer, G. L., Falke, J. J., & Parkinson, J. S. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.014 · Cited by 632 · see citing works
Molecular Mechanisms of Two-Component Signal Transduction
Zschiedrich, C. P., Keidel, V., & Szurmant, H. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.003 · Cited by 540 · see citing works
Homeoviscous Adaptation and the Regulation of Membrane Lipids
Ernst, R., Ejsing, C. S., & Antonny, B. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.08.013 · Cited by 506 · see citing works
Peptide Signaling in the Staphylococci
Thoendel, M., Kavanaugh, J. S., Flack, C. E., & Horswill, A. R. (2010) · Chemical Reviews · doi:10.1021/cr100370n · Cited by 437 · see citing works
Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update
Parkinson, J. S., Hazelbauer, G. L., & Falke, J. J. (2015) · Trends in Microbiology · doi:10.1016/j.tim.2015.03.003 · Cited by 414 · see citing works
Casino, P., Rubio, V., & Marina, A. (2009) · Cell · doi:10.1016/j.cell.2009.08.032 · Cited by 382 · see citing works
Howden, B. P., McEvoy, C. R. E., Allen, D. L., Chua, K., Gao, W., Harrison, P. F., Bell, J. M., Coombs, G. W., Bennett-Wood, V. R., Porter, J. L., et al. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002359 · Cited by 371 · see citing works
Design and Signaling Mechanism of Light-Regulated Histidine Kinases
Möglich, A., Ayers, R. A., & Moffat, K. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.12.017 · Cited by 341 · see citing works
Universal architecture of bacterial chemoreceptor arrays
Briegel, A., Ortega, D. R., Tocheva, E. I., Wuichet, K., Li, Z., Chen, S., Müller, A., Iancu, C. V., Murphy, G. E., Dobro, M. J., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905181106 · Cited by 328 · see citing works
Structural insights into the signalling mechanisms of two-component systems
Jacob‐Dubuisson, F., Méchaly, A., Betton, J., & Antoine, R. (2018) · Nature Reviews Microbiology · doi:10.1038/s41579-018-0055-7 · Cited by 310 · see citing works
Newell, P. D., Monds, R. D., & O’Toole, G. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808933106 · Cited by 292 · see citing works
Signal Transduction in Histidine Kinases: Insights from New Structures
Bhate, M., Molnar, K. S., Goulian, M., & DeGrado, W. F. (2015) · Structure · doi:10.1016/j.str.2015.04.002 · Cited by 284 · see citing works
Alexander, R. P., & Zhulin, I. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609359104 · Cited by 268 · see citing works
Yoon, E.-J., Courvalin, P. M., & Grillot‐Courvalin, C. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.02556-12 · Cited by 257 · see citing works
The mechanism of signal transduction by two-component systems
Casino, P., Rubio, V., & Marina, A. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.09.010 · Cited by 256 · see citing works
Structure and Functional Role of Dynein's Microtubule-Binding Domain
Carter, A. P., Garbarino, J. E., Kubalek, E. W., Shipley, W. E., Cho, C., Milligan, R. A., Vale, R. D., & Gibbons, I. R. (2008) · Science · doi:10.1126/science.1164424 · Cited by 248 · see citing works
Stimulus sensing and signal processing in bacterial chemotaxis
Bi, S., & Sourjik, V. (2018) · Current Opinion in Microbiology · doi:10.1016/j.mib.2018.02.002 · Cited by 248 · see citing works
Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea
Ud-Din, A. I. M. S., & Roujeinikova, A. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2514-0 · Cited by 222 · see citing works
Bacterial phytochromes: More than meets the light
Auldridge, M. E., & Forest, K. T. (2011) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.546389 · Cited by 223 · see citing works
Engineered photoreceptors as novel optogenetic tools
Möglich, A., & Moffat, K. (2010) · Photochemical & Photobiological Sciences · doi:10.1039/c0pp00167h · Cited by 223 · see citing works
Coiled Coils – A Model System for the 21st Century
Lupas, A. N., & Baßler, J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.10.007 · Cited by 199 · see citing works
Self-citationStructural Basis for c-di-GMP-Mediated Inside-Out Signaling Controlling Periplasmic Proteolysis
Navarro, M. V. A. S., Newell, P. D., Krasteva, P. V., Chatterjee, D., Madden, D. R., O’Toole, G. A., & Sondermann, H. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000588 · Cited by 192 · see citing works
Signaling Mechanisms of HAMP Domains in Chemoreceptors and Sensor Kinases
Parkinson, J. S. (2010) · Annual Review of Microbiology · doi:10.1146/annurev.micro.112408.134215 · Cited by 192 · see citing works
Structural plasticity and catalysis regulation of a thermosensor histidine kinase
Albanesi, D., Martín, M., Trajtenberg, F., Mansilla, M. C., Haouz, A., Alzari, P. M., de Mendoza, D., & Buschiazzo, A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906699106 · Cited by 187 · see citing works
Diensthuber, R. P., Bommer, M., Gleichmann, T., & Möglich, A. (2013) · Structure · doi:10.1016/j.str.2013.04.024 · Cited by 184 · see citing works
Chun, C. D., Liu, O. W., & Madhani, H. D. (2007) · PLoS Pathogens · doi:10.1371/journal.ppat.0030022 · Cited by 181 · see citing works
Mechanism of transmembrane signaling by sensor histidine kinases
Gushchin, I., Melnikov, I., Polovinkin, V., Ishchenko, A., Yuzhakova, A., Buslaev, P., Bourenkov, G. P., Grudinin, S., Round, E. S., Balandin, T. G., et al. (2017) · Science · doi:10.1126/science.aah6345 · Cited by 175 · see citing works
Wang, C., Sang, J., Wang, J., Su, M.-Y., Downey, J. S., Wu, Q., Wang, S., Cai, Y., Xu, X., Wu, J., et al. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001493 · Cited by 167 · see citing works
A brief history of de novo protein design: minimal, rational, and computational.
Woolfson, D. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167160 · Cited by 139 · see citing works
Engineering of a red-light–activated human cAMP/cGMP-specific phosphodiesterase
Gasser, C., Taiber, S., Yeh, C.-M., Wittig, C. H., Hegemann, P., Ryu, S., Wunder, F., & Möglich, A. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321600111 · Cited by 165 · see citing works
Structure of Concatenated HAMP Domains Provides a Mechanism for Signal Transduction
Airola, M. V., Watts, K. J., Bilwes, A. M., & Crane, B. R. (2010) · Structure · doi:10.1016/j.str.2010.01.013 · Cited by 145 · see citing works
Qian, X., Gunturu, S., Guo, J., Chai, B., Cole, J. R., Gu, J., & Tiedje, J. M. (2021) · Microbiome · doi:10.1186/s40168-021-01047-4 · Cited by 140 · see citing works
A Eukaryotic Sensor for Membrane Lipid Saturation
Covino, R., Ballweg, S., Stordeur, C., Michaelis, J. B., Puth, K., Wernig, F., Bahrami, A. H., Ernst, A. M., Hummer, G., & Ernst, R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.015 · Cited by 139 · see citing works
Zhou, Q., Ames, P., & Parkinson, J. S. (2009) · Molecular Microbiology · doi:10.1111/j.1365-2958.2009.06819.x · Cited by 138 · see citing works
PhoP, a key player in Mycobacterium tuberculosis virulence
Ryndak, M. B., Wang, S., & Smith, I. (2008) · Trends in Microbiology · doi:10.1016/j.tim.2008.08.006 · Cited by 137 · see citing works
A Ligand-Induced Switch in the Periplasmic Domain of Sensor Histidine Kinase CitA
Sevvana, M., Vijayan, V., Zweckstetter, M., Reinelt, S., Madden, D. R., Herbst‐Irmer, R., Sheldrick, G. M., Bott, M. H., Griesinger, C., & Becker, S. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.01.024 · Cited by 134 · see citing works
Chemotaxis-Like Regulatory Systems: Unique Roles in Diverse Bacteria
Kirby, J. R. (2009) · Annual Review of Microbiology · doi:10.1146/annurev.micro.091208.073221 · Cited by 133 · see citing works
Wuichet, K., Alexander, R. P., & Zhulin, I. B. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)22001-9 · Cited by 131 · see citing works
Stress Sensors and Signal Transducers in Cyanobacteria
Los, D. A., Zorina, A. A., Sinetova, M. A., Kryazhov, S., Mironov, K. S., & Зинченко, В. В. (2010) · Sensors · doi:10.3390/s100302386 · Cited by 130 · see citing works
Sensor complexes regulating two-component signal transduction
Szurmant, H., White, R. A., & Hoch, J. A. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.08.019 · Cited by 129 · see citing works
Long-range allosteric signaling in red light–regulated diguanylyl cyclases
Gourinchas, G., Etzl, S., Göbl, C., Vide, U., Madl, T., & Winkler, A. (2017) · Science Advances · doi:10.1126/sciadv.1602498 · Cited by 124 · see citing works
Bacterial chemoreceptors: providing enhanced features to two-component signaling
Hazelbauer, G. L., & Lai, W. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.12.014 · Cited by 123 · see citing works
Dynamic Helix Interactions in Transmembrane Signaling
Matthews, E. E., Zoonens, M. A., & Engelman, D. M. (2006) · Cell · doi:10.1016/j.cell.2006.10.016 · Cited by 121 · see citing works
Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation
Méchaly, A., Sassoon, N., Betton, J., & Alzari, P. M. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001776 · Cited by 118 · see citing works
Stress-Induced Remodeling of the Bacterial Proteome
Guo, M. S., & Gross, C. A. (2014) · Current Biology · doi:10.1016/j.cub.2014.03.023 · Cited by 114 · see citing works
EnvZ/OmpR Two-Component Signaling: An Archetype System That Can Function Noncanonically
Kenney, L. J., & Anand, G. S. (2020) · EcoSal Plus · doi:10.1128/ecosalplus.esp-0001-2019 · Cited by 117 · see citing works
Molnar, K. S., Bonomi, M., Pellarin, R., Clinthorne, G. D., González, G., Goldberg, S. D., Goulian, M., Šali, A., & DeGrado, W. F. (2014) · Structure · doi:10.1016/j.str.2014.04.019 · Cited by 116 · see citing works
Engineering adenylate cyclases regulated by near-infrared window light
Ryu, M., Kang, I.-H., Nelson, M. D., Jensen, T. M., Lyuksyutova, A. I., Siltberg-Liberles, J., Raizen, D. M., & Gomelsky, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1324301111 · Cited by 116 · see citing works
The Structure and Topology of α-Helical Coiled Coils
Lupas, A. N., Baßler, J., & Dunin-Horkawicz, S. (2017) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-319-49674-0_4 · Cited by 116 · see citing works
Self-citationGrote, M., Engelhard, M., & Hegemann, P. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.08.006 · Cited by 110 · see citing works
Regulation of innate immune responses by transmembrane interactions: Lessons from the TLR family
Reuven, E. M., Fink, A., & Shai, Y. (2014) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2014.01.020 · Cited by 110 · see citing works
Huang, J., Li, C., Song, J., Velkov, T., Wang, L., Zhu, Y., & Li, J. (2020) · Future Microbiology · doi:10.2217/fmb-2019-0322 · Cited by 109 · see citing works
Understanding a protein fold: The physics, chemistry, and biology of α-helical coiled coils
Woolfson, D. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104579 · Cited by 106 · see citing works
“…been proposed, structural studies of an archaeal HAMP suggest that a ‘ gearbox ’ mechanism could be a play in which alternate coiled-coil core-packing arrangements drive the helices to rotate about their long axes to generate a rotational signal that is passed to the intracellular components (273).”
The Mechanisms of HAMP-Mediated Signaling in Transmembrane Receptors
Ferris, H. U., Dunin-Horkawicz, S., Mondéjar, L. G., Hulko, M., Hantke, K., Martin, J., Schultz, J. E., Zeth, K., Lupas, A. N., & Coles, M. P. (2011) · Structure · doi:10.1016/j.str.2011.01.006 · Cited by 104 · see citing works
Self-citationVertebrate Membrane Proteins: Structure, Function, and Insights from Biophysical Approaches
Müller, D. J., Wu, N., & Palczewski, K. (2008) · Pharmacological Reviews · doi:10.1124/pr.107.07111 · Cited by 104 · see citing works
Mechanism of Regulation of Receptor Histidine Kinases
Ferris, H. U., Dunin-Horkawicz, S., Hornig, N., Hulko, M., Martin, J., Schultz, J. E., Zeth, K., Lupas, A. N., & Coles, M. P. (2012) · Structure · doi:10.1016/j.str.2011.11.014 · Cited by 102 · see citing works
Self-citationMicrobial Rhodopsins: Scaffolds for Ion Pumps, Channels, and Sensors
Klare, J. P., Chizhov, I. V., & Engelhard, M. (2007) · Springer eBooks · doi:10.1007/400_2007_041 · Cited by 102 · see citing works
Comprehensive Analysis of HAMP Domains: Implications for Transmembrane Signal Transduction
Dunin-Horkawicz, S., & Lupas, A. N. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.02.031 · Cited by 102 · see citing works
Self-citationSite-directed spin labeling EPR spectroscopy in protein research
Klare, J. P. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0155 · Cited by 100 · see citing works
Aer on the inside looking out: paradigm for a PAS–HAMP role in sensing oxygen, redox and energy
Taylor, B. L. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05889.x · Cited by 99 · see citing works
Swain, K. E., Gonzalez, M. A., & Falke, J. J. (2009) · Biochemistry · doi:10.1021/bi901020d · Cited by 99 · see citing works
Structural Information from Spin-Labels and Intrinsic Paramagnetic Centres in the Biosciences
Timmel, C. R., & Harmer, J. R. (2013) · Structure and bonding · doi:10.1007/978-3-642-39125-5 · Cited by 90 · see citing works
Physical Responses of Bacterial Chemoreceptors
Vaknin, A., & Berg, H. C. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.12.024 · Cited by 90 · see citing works
Biphasic control logic of HAMP domain signalling in the Escherichia coli serine chemoreceptor
Zhou, Q., Ames, P., & Parkinson, J. S. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2011.07577.x · Cited by 89 · see citing works
Li, X., Fleetwood, A. D., Bayas, C. A., Bilwes, A. M., Ortega, D. R., Falke, J. J., Zhulin, I. B., & Crane, B. R. (2013) · Biochemistry · doi:10.1021/bi400383e · Cited by 87 · see citing works
Hybrid histidine kinases in pathogenic fungi
Defosse, T. A., Sharma, A., Mondal, A. K., de Bernonville, T. D., Latgé, J., Calderone, R., Giglioli‐Guivarc’h, N., Courdavault, V., Clastre, M., & Papon, N. (2015) · Molecular Microbiology · doi:10.1111/mmi.12911 · Cited by 87 · see citing works
Yoshida, K., Tsunoda, S. P., Brown, L. S., & Kandori, H. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.775569 · Cited by 85 · see citing works
Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors
Khursigara, C. M., Wu, X., Zhang, P., Lefman, J., & Subramaniam, S. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806401105 · Cited by 85 · see citing works
Fillinger, S., Ajouz, S., Nicot, P. C., Leroux, P., & Bardin, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042520 · Cited by 85 · see citing works
Bass, R. B., Butler, S. L., Chervitz, S. A., Gloor, S. L., & Falke, J. J. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)23002-2 · Cited by 84 · see citing works
Hu, J., Zhang, X., Liu, X., Chen, C., & Sun, B. (2014) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.04290-14 · Cited by 83 · see citing works
Szurmant, H., Bu, L., Brooks, C. L., & Hoch, J. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800247105 · Cited by 83 · see citing works
Adenylate cyclases: Receivers, transducers, and generators of signals
Baßler, J., Schultz, J. E., & Lupas, A. N. (2018) · Cellular Signalling · doi:10.1016/j.cellsig.2018.03.002 · Cited by 82 · see citing works
Self-citationWorkentine, M. L., Chang, L., Ceri, H., & Turner, R. J. (2009) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2008.01445.x · Cited by 81 · see citing works
Complete structure of the chemosensory array core signalling unit in an E. coli minicell strain
Burt, A., Cassidy, C. K., Ames, P., Bacia‐Verloop, M., Baulard, M., Huard, K., Luthey-Schulten, Z. A., Desfosses, A., Stansfeld, P. J., Margolin, W., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-14350-9 · Cited by 80 · see citing works
Burroughs, A. M., & Aravind, L. (2020) · Journal of Bacteriology · doi:10.1128/jb.00365-20 · Cited by 80 · see citing works
C4-Dicarboxylates Sensing Mechanism Revealed by the Crystal Structures of DctB Sensor Domain
Zhou, Y.-F., Nan, B., Nan, J., Ma, Q., Panjikar, S., Liang, Y., Wang, Y., & Su, X. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.08.010 · Cited by 78 · see citing works
Otero, L. H., Klinke, S., Rinaldi, J., Escobar, F. V., Mroginski, M. A., López, M. F., Malamud, F., Vojnov, A. A., Hildebrandt, P., Goldbaum, F. A., et al. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.04.012 · Cited by 78 · see citing works
Cyclic AMP signalling in mycobacteria: redirecting the conversation with a common currency
Bai, G., Knapp, G. S., & McDonough, K. A. (2010) · Cellular Microbiology · doi:10.1111/j.1462-5822.2010.01562.x · Cited by 77 · see citing works
Bacterial chemoreceptors and chemoeffectors
Bi, S., & Lai, L. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1770-5 · Cited by 76 · see citing works
Signal transduction in photoreceptor histidine kinases
Möglich, A. (2019) · Protein Science · doi:10.1002/pro.3705 · Cited by 74 · see citing works
Bhatnagar, J., Borbat, P. P., Pollard, A. M., Bilwes, A. M., Freed, J. H., & Crane, B. R. (2010) · Biochemistry · doi:10.1021/bi100055m · Cited by 74 · see citing works
Bacterial transmembrane signalling systems and their engineering for biosensing
Jung, K., Fabiani, F. D., Hoyer, E. A., & Lassak, J. (2018) · Open Biology · doi:10.1098/rsob.180023 · Cited by 74 · see citing works
Protein histidine kinases: assembly of active sites and their regulation in signaling pathways
Stewart, R. C. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2009.12.013 · Cited by 74 · see citing works
Meena, N. P., Kaur, H., & Mondal, A. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.075721 · Cited by 71 · see citing works
An Asymmetry-to-Symmetry Switch in Signal Transmission by the Histidine Kinase Receptor for TMAO
Moore, J. O., & Hendrickson, W. A. (2012) · Structure · doi:10.1016/j.str.2012.02.021 · Cited by 70 · see citing works
Leng, Y., Vakulskas, C. A., Zere, T., Pickering, B., Watnick, P. I., Babitzke, P., & Romeo, T. (2015) · Molecular Microbiology · doi:10.1111/mmi.13259 · Cited by 68 · see citing works
HAMP Domain Conformers That Propagate Opposite Signals in Bacterial Chemoreceptors
Airola, M. V., Sukomon, N., Samanta, D., Borbat, P. P., Freed, J. H., Watts, K. J., & Crane, B. R. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001479 · Cited by 68 · see citing works
Ng, W., Wei, Y., Perez, L. J., Cong, J.-P., Long, T., Koch, M., Semmelhack, M. F., Wingreen, N. S., & Bassler, B. L. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001392107 · Cited by 67 · see citing works
Colonization of biofilm in wastewater treatment: A review
Li, L., He, Z., Liang, T., Sheng, T., Zhang, F., Wu, D., & Ma, F. (2021) · Environmental Pollution · doi:10.1016/j.envpol.2021.118514 · Cited by 65 · see citing works
Firon, A., Tazi, A., Cunha, V. D., Brinster, S., Sauvage, E., Dramsi, S., Golenbock, D. T., Glaser, P., Poyart, C., & Trieu‐Cuot, P. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003179 · Cited by 65 · see citing works
Phenol Sensing by Escherichia coli Chemoreceptors: a Nonclassical Mechanism
Pham, H. T., & Parkinson, J. S. (2011) · Journal of Bacteriology · doi:10.1128/jb.05987-11 · Cited by 65 · see citing works
Ma, X., Beuve, A. V., & van den Akker, F. (2010) · BMC Structural Biology · doi:10.1186/1472-6807-10-2 · Cited by 63 · see citing works
Haneburger, I., Eichinger, A., Skerra, A., & Jung, K. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.196923 · Cited by 63 · see citing works
Ames, P., Zhou, Q., & Parkinson, J. S. (2008) · Journal of Bacteriology · doi:10.1128/jb.00750-08 · Cited by 62 · see citing works
Signal Transfer in Haloarchaeal Sensory Rhodopsin– Transducer Complexes†
Sasaki, J., & Spudich, J. L. (2008) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2008.00314.x · Cited by 62 · see citing works
Transmembrane Signal Transduction in Two‐Component Systems: Piston, Scissoring, or Helical Rotation?
Gushchin, I., & Gordeliy, V. (2017) · BioEssays · doi:10.1002/bies.201700197 · Cited by 60 · see citing works
Engineering Bacterial Signals and Sensors
Salis, H. M., Tamsir, A., & Voigt, C. A. (2009) · Contributions to microbiology · doi:10.1159/000219381 · Cited by 56 · see citing works
Structural Analysis of Sensor Domains from the TMAO-Responsive Histidine Kinase Receptor TorS
Moore, J. O., & Hendrickson, W. A. (2009) · Structure · doi:10.1016/j.str.2009.07.015 · Cited by 57 · see citing works
- Authors
- Hulko, M., Berndt, F., Gruber, M., Linder, J. U., Truffault, V., Schultz, A., Martin, J., Schultz, J. E., Lupas, A. N., & Coles, M.
- Affiliations
- Max Planck Institute for Developmental Biology (DE)
- University of Tübingen (DE)
- Corresponding author
- Lupas, Andrei N.
- ORCID
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2006-09
- Volume
- 126
- Issue
- 5
- Pages
- 929-940
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2068254342
- Cited by
- 416
- References
- 46
- Citations by year
- 2026: 11 · 2025: 8 · 2024: 7 · 2023: 9 · 2022: 6 · 2021: 23 · 2020: 19 · 2019: 15 · 2018: 16 · 2017: 27 · 2016: 18 · 2015: 18 · 2014: 36 · 2013: 30 · 2012: 19
- FWCI
- 11.75
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2511 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- HAMP domain, helix rotation, transmembrane signaling, signal transduction, coiled coil, histidine kinase, adenylate cyclase, chemotaxis receptor, homodimer, side chain size, conformational equilibrium, protein structure
- MeSH terms
- Adenosine Triphosphate, Adenylyl Cyclases, Amino Acid Sequence, Bacterial Proteins, Chemoreceptor Cells, Chemotaxis, Escherichia coli, Membrane Proteins, Models, Molecular, Molecular Sequence Data, Mutation, Protein Denaturation, Receptors, Cell Surface, Recombinant Fusion Proteins, Signal Transduction, Protein Structure, Tertiary, Archaeoglobus fulgidus, Archaeal Proteins, Nuclear Magnetic Resonance, Biomolecular, Catalytic Domain, Escherichia coli Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review