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Structures of the Bacterial Ribosome at 3.5 Å Resolution
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We describe two structures of the intact bacterial ribosome from Escherichia coli determined to a resolution of 3.5 angstroms by x-ray crystallography. These structures provide a detailed view of the interface between the small and large ribosomal subunits and the conformation of the peptidyl transferase center in the context of the intact ribosome. Differences between the two ribosomes reveal a high degree of flexibility between the head and the rest of the small subunit. Swiveling of the head of the small subunit observed in the present structures, coupled to the ratchet-like motion of the two subunits observed previously, suggests a mechanism for the final movements of messenger RNA (mRNA) and transfer RNAs (tRNAs) during translocation.
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Citations
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
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Crystal structure of the ribosome at 5.5 Å resolution
Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F. (2001) · Science · doi:10.1126/science.1060089 · Cited by 1,944
Self-citationStructure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., et al. (2000) · Cell · doi:10.1016/s0092-8674(00)00084-2 · Cited by 979
The ribosome as an entropy trap
Sievers, A., Beringer, M., Rodnina, M. V., & Wolfenden, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402488101 · Cited by 357
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The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech, T. R., & Steitz, J. A. (2014) · Cell · doi:10.1016/j.cell.2014.03.008 · Cited by 2,524
Unusual biology across a group comprising more than 15% of domain Bacteria
Brown, C. T., Hug, L. A., Thomas, B. C., Sharon, I., Castelle, C. J., Singh, A., Wilkins, M. J., Wrighton, K. C., Williams, K. H., & Banfield, J. F. (2015) · Nature · doi:10.1038/nature14486 · Cited by 1,216
Ribosome-targeting antibiotics and mechanisms of bacterial resistance
Wilson, D. N. (2014) · Nature Reviews Microbiology · doi:10.1038/nrmicro3155 · Cited by 1,054
Sensitivity and correlation of hypervariable regions in 16S rRNA genes in phylogenetic analysis
Yang, B., Wang, Y., & Qian, P.-Y. (2016) · BMC Bioinformatics · doi:10.1186/s12859-016-0992-y · Cited by 560
Computed structures of core eukaryotic protein complexes
Humphreys, I. R., Pei, J., Baek, M., Krishnakumar, A., Anishchenko, I., Ovchinnikov, S., Zhang, J., Ness, T. J., Banjade, S., Bagde, S. R., et al. (2021) · Science · doi:10.1126/science.abm4805 · Cited by 542
The Structure of the Ribosome with Elongation Factor G Trapped in the Posttranslocational State
Gao, Y.-G., Selmer, M., Dunham, C. M., Weixlbaumer, A., Kelley, A. C., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179709 · Cited by 513
Crystal Structure of a 70S Ribosome-tRNA Complex Reveals Functional Interactions and Rearrangements
Korostelev, A., Trakhanov, S., Laurberg, M., & Noller, H. F. (2006) · Cell · doi:10.1016/j.cell.2006.08.032 · Cited by 498
One core, two shells: bacterial and eukaryotic ribosomes
Melnikov, S., Ben-Shem, A., Garreau de Loubresse, N., Jenner, L., Yusupova, G., & Yusupov, M. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2313 · Cited by 477
A Role for Codon Order in Translation Dynamics
Cannarozzi, G., Schraudolph, N. N., Faty, M., von Rohr, P., Friberg, M. T., Roth, A. C., Gonnet, P., Gonnet, G., & Barral, Y. (2010) · Cell · doi:10.1016/j.cell.2010.02.036 · Cited by 354
Toh, S., Xiong, L., Arias, C. A., Villegas, M. V., Lolans, K., Quinn, J., & Mankin, A. S. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05744.x · Cited by 338
History of the ribosome and the origin of translation
Petrov, A. S., Gulen, B., Norris, A. M., Kovacs, N. A., Bernier, C. R., Lanier, K. A., Fox, G. E., Harvey, S. C., Wartell, R. M., Hud, N. V., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509761112 · Cited by 290
Coupling of Ribosomal L1 Stalk and tRNA Dynamics during Translation Elongation
Fei, J., Kosuri, P., MacDougall, D. D., & Gonzalez, R. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.012 · Cited by 316
The native 3D organization of bacterial polysomes
Brandt, F., Etchells, S. A., Ortiz, J. O., Elcock, A. H., Hartl, F. U., & Baumeister, W. (2009) · Cell · doi:10.1016/j.cell.2008.11.016 · Cited by 258
Molecular Mechanism of Drug-Dependent Ribosome Stalling
Vazquez-Laslop, N., Thum, C., & Mankin, A. S. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.026 · Cited by 260
Origin and evolution of the ribosome
Fox, G. E. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003483 · Cited by 258
Crystal structures of EF-G-ribosome complexes trapped in intermediate states of translocation
Zhou, J., Lancaster, L., Donohue, J. P., & Noller, H. F. (2013) · Science · doi:10.1126/science.1236086 · Cited by 229
A hierarchical model for evolution of 23S ribosomal RNA
Bokov, K., & Steinberg, S. V. (2009) · Nature · doi:10.1038/nature07749 · Cited by 228
Structural basis for TetM-mediated tetracycline resistance
Dönhöfer, A., Franckenberg, S., Wickles, S., Berninghausen, O., Beckmann, R., & Wilson, D. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208037109 · Cited by 217
Root of the Tree: The Significance, Evolution, and Origins of the Ribosome
Bowman, J. C., Petrov, A. S., Frenkel-Pinter, M., Penev, P. I., & Williams, L. D. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00742 · Cited by 197
Taylor, D. J., Nilsson, J., Merrill, A. R., Andersen, G. R., Nissen, P., & Frank, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601677 · Cited by 193
The Ribosomal Peptidyl Transferase
Beringer, M., & Rodnina, M. V. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.015 · Cited by 172
SecM-Stalled Ribosomes Adopt an Altered Geometry at the Peptidyl Transferase Center
Bhushan, S., Hoffmann, T., Seidelt, B., Frauenfeld, J., Mielke, T., Berninghausen, O., Wilson, D. N., & Beckmann, R. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000581 · Cited by 154
Structure of the E. coli signal recognition particle bound to a translating ribosome.
Schaffitzel, C., Oswald, M., Berger, I., Ishikawa, T., Abrahams, J. P., Koerten, H. K., Koning, R. I., & Ban, N. (2006) · Nature · doi:10.1038/nature05182 · Cited by 136
When Too Much ATP Is Bad for Protein Synthesis
Pontes, M. H., Sevostyanova, A., & Groisman, E. A. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.06.021 · Cited by 134
Reducing Ribosome Biosynthesis Promotes Translation during Low Mg 2+ Stress
Pontes, M. H., Yeom, J., & Groisman, E. A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.008 · Cited by 115
Mg 2+ , K + , and the Ribosome
Nierhaus, K. H. (2014) · Journal of Bacteriology · doi:10.1128/jb.02297-14 · Cited by 123
SecA interacts with ribosomes in order to facilitate posttranslational translocation in bacteria.
Huber, D., Rajagopalan, N., Preissler, S., Rocco, M. A., Merz, F., Kramer, G., & Bukau, B. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.028 · Cited by 109
‘Entropy-Based mechanism of ribosome-nucleoid segregation in E. coli cells’
Mondal, J., Bratton, B. P., Li, Y., Yethiraj, A., & Weisshaar, J. C. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.04.030 · Cited by 110
The origin and evolution of the ribosome
Smith, T. F., Lee, J. C., Gutell, R. R., & Hartman, H. (2008) · Biology Direct · doi:10.1186/1745-6150-3-16 · Cited by 85
Camprubí, E., de Leeuw, J. W., House, C. H., Raulin, F., Russell, M. J., Spang, A., Tirumalai, M. R., & Westall, F. (2019) · Space Science Reviews · doi:10.1007/s11214-019-0624-8 · Cited by 84
“…the LSU is the RNA (Cate et al. 1999; Ban et al. 2000; Nissen et al. 2000; Harms et al. 2001; Schlunzen et al. 2001; Spahn et al. 2001; Yusupov et al. 2001; Hansen et al. 2002; Ramakrishnan 2002; Schuwirth et al. 2005; Selmer et al. 2006; Armache et al. 2010; Jenner et al. 2012; Anger et al. 2013).”
BackgroundRibosomal proteins: Structure, function, and evolution
Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060028 · Cited by 63
Multiple prebiotic metals mediate translation
Bray, M. S., Lenz, T. K., Haynes, J. W., Bowman, J. C., Petrov, A. S., Reddi, A. R., Hud, N. V., Williams, L. D., & Glass, J. B. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1803636115 · Cited by 58
Cocozaki, A. I., Altman, R. B., Huang, J., Buurman, E. T., Kazmirski, S. L., Doig, P., Prince, D. B., Blanchard, S. C., Cate, J. H. D., & Ferguson, A. D. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605127113 · Cited by 56
Self-citationThe Peptidyl Transferase Center: a Window to the Past
Tirumalai, M. R., Rivas, M., Tran, Q., & Fox, G. E. (2021) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00104-21 · Cited by 53
A viral ADP-ribosyltransferase attaches RNA chains to host proteins
Wolfram-Schauerte, M., Pozhydaieva, N., Grawenhoff, J., Welp, L. M., Silbern, I., Wulf, A., Billau, F. A., Glatter, T., Urlaub, H., Jäschke, A., et al. (2023) · Nature · doi:10.1038/s41586-023-06429-2 · Cited by 53
Kirthi, N., Roy-Chaudhuri, B., Kelley, T., & Culver, G. M. (2006) · RNA · doi:10.1261/rna.302006 · Cited by 46
Modulating co-translational protein folding by rational design and ribosome engineering
Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45
Obana, N., Takada, H., Crowe-McAuliffe, C., Iwamoto, M., Egorov, A. A., Wu, K. J. Y., Chiba, S., Murina, V., Paternoga, H., Tresco, B. I. C., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad193 · Cited by 42
Molecular dynamics of EF‐G during translocation
Li, W., Trabuco, L. G., Schulten, K., & Frank, J. (2011) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.22976 · Cited by 38
Lawrence, M. G., Shamsuzzaman, M., Kondopaka, M., Pascual, C., Zengel, J. M., & Lindahl, L. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw493 · Cited by 36
Diverse relationships between metal ions and the ribosome
Akanuma, G. (2021) · Bioscience, Biotechnology, and Biochemistry · doi:10.1093/bbb/zbab070 · Cited by 34
Mutagenesis of the modified bases, m5U1939 and ψ2504, in Escherichia coli 23S rRNA
Persaud, C., Lu, Y., Vila-Sanjurjo, A., Campbell, J. L., Finley, J., & O’Connor, M. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.021 · Cited by 33
Self-citationRNA language models predict mutations that improve RNA function
Shulgina, Y., Trinidad, M. I., Langeberg, C. J., Nisonoff, H., Chithrananda, S., Skopintsev, P., Nissley, A. J., Patel, J., Boger, R. S., Shi, H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54812-y · Cited by 32
Self-citationAkanuma, G., Yamazaki, K., Yagishi, Y., Iizuka, Y., Ishizuka, M., Kawamura, F., & Kato-Yamada, Y. (2018) · Journal of Bacteriology · doi:10.1128/jb.00212-18 · Cited by 27
The Ribosome: Some Hard Facts about Its Structure and Hot Air about Its Evolution
Ramakrishnan, V. (2009) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2009.74.032 · Cited by 27
Lomakin, I. B., Devarkar, S. C., Patel, S., Grada, A., & Bunick, C. G. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad103 · Cited by 25
Physiological cost of antibiotic resistance: Insights from a ribosome variant in bacteria
Moon, E. C., Modi, T., Lee, D.-Y. D., Yangaliev, D., Garcia-Ojalvo, J., Ozkan, S. B., & Süel, G. M. (2024) · Science Advances · doi:10.1126/sciadv.adq5249 · Cited by 9
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Zhang, W., Sun, C., Xu, Z., & Xu, W. (2025) · Analytical Chemistry · doi:10.1021/acs.analchem.5c01431 · Cited by 3
Self-citation
Metadata
- Authors
- Schuwirth, B. S., Borovinskaya, M. A., Hau, C. W., Zhang, W., Vila-Sanjurjo, A., Holton, J. M., & Cate, J. H. D.
- Venue
- Science
- Published
- 2005-11-04
- Volume
- 310
- Issue
- 5749
- Pages
- 827-834
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073149987
- Cited by
- 1,418
- References
- 5
- FWCI
- 39.76
- Type
- journal article
- Language
- en
- Open access
- green
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