Cited by 1,000RNA and protein synthesis mechanismsRNA modifications and cancerEnzyme Structure and Function

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Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

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Schluenzen, Frank, Tocilj, Ante, Zarivach, Raz, Harms, Joerg, Gluehmann, Marco, Janell, Daniela, Bashan, Anat, Bartels, Heike, Agmon, Ilana, Franceschi, François, Yonath, Ada·2000·Cell

DOI 10.1016/s0092-8674(00)00084-2

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Abstract

The small ribosomal subunit performs the decoding of genetic information during translation. The structure of that from Thermus thermophilus shows that the decoding center, which positions mRNA and three tRNAs, is constructed entirely of RNA. The entrance to the mRNA channel will encircle the message when a latch-like contact closes and contributes to processivity and fidelity. Extended RNA helical elements that run longitudinally through the body transmit structural changes, correlating events at the particle's far end with the cycle of mRNA translocation at the decoding region. 96% of the nucleotides were traced and the main fold of all proteins was determined. The latter are either peripheral or appear to serve as linkers. Some may assist the directionality of translocation.

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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
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
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 15,723
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
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 1,892
Methods used in the structure determination of bovine mitochondrial F1 ATPase
Abrahams, J. P., & Leslie, A. G. W. (1996) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444995008754 · Cited by 1,090
Efficient anisotropic refinement of macromolecular structures using FFT
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., & Dodson, E. J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499801405x · Cited by 937
Structure, Function, and Genetics of Ribosomes
Hardesty, B., & Kramer, G. (1986) · Springer series in molecular biology · doi:10.1007/978-1-4612-4884-2 · Cited by 852
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Frank, J., & Agrawal, R. K. (2000) · Nature · doi:10.1038/35018597 · Cited by 799
X-ray Crystal Structures of 70 S Ribosome Functional Complexes
Cate, J. H. D., Yusupov, M., Yusupova, G. Z., Earnest, T. N., & Noller, H. F. (1999) · Science · doi:10.1126/science.285.5436.2095 · Cited by 583

Show all 72 references

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Schlünzen, F., Zarivach, R., Harms, J., Bashan, A., Tocilj, A., Albrecht, R., Yonath, A., & Franceschi, F. J. (2001) · Nature · doi:10.1038/35101544 · Cited by 1,057
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Versatility of Aminoglycosides and Prospects for Their Future
Vakulenko, S. B., & Mobashery, S. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.3.430-450.2003 · Cited by 641
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Laursen, B. S., Sørensen, H. P., Mortensen, K. K., & Petersen, H. U. (2005) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.69.1.101-123.2005 · Cited by 621
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Bagley, M. C., Dale, J. W., Merritt, E. A., & Xiong, X. (2005) · Chemical Reviews · doi:10.1021/cr0300441 · Cited by 612
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Wilson, D. N., & Cate, J. H. D. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a011536 · Cited by 508
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Spahn, C. M. T., Kieft, J. S., Grassucci, R. A., Penczek, P. A., Zhou, K., Doudna, J. A., & Frank, J. (2001) · Science · doi:10.1126/science.1058409 · Cited by 470
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Blanchard, S. C., Kim, H. D., Gonzalez, R. L., Puglisi, J. D., & Chu, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403884101 · Cited by 469
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Connell, S. R., Tracz, D. M., Nierhaus, K. H., & Taylor, D. E. (2003) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.47.12.3675-3681.2003 · Cited by 449
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Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation
Spahn, C. M. T., Gómez-Lorenzo, M. G., Grassucci, R. A., Jørgensen, R., Andersen, G. R., Beckmann, R., Penczek, P. A., Ballesta, J. P. G., & Frank, J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600102 · Cited by 385
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Zaher, H. S., & Green, R. (2009) · Cell · doi:10.1016/j.cell.2009.01.036 · Cited by 381
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Mathews, D. H., & Turner, D. H. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5351 · Cited by 379
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Crystal structure of the 30 s ribosomal subunit from Thermus thermophilus: structure of the proteins and their interactions with 16 s RNA
Brodersen, D. E., Clemons, W., Carter, A. P., Wimberly, B. T., & Ramakrishnan, V. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5359 · Cited by 363
Comparative analysis of ribosomal proteins in complete genomes: an example of reductive evolution at the domain scale
Lecompte, O. (2002) · Nucleic Acids Research · doi:10.1093/nar/gkf693 · Cited by 352
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Noller, H. F. (2005) · Science · doi:10.1126/science.1111771 · Cited by 345
Elucidation of the molecular structures of components of the phycobilisome: reconstructing a giant
Adir, N. (2005) · Photosynthesis Research · doi:10.1007/s11120-004-2143-y · Cited by 340
Structure of a yeast spliceosome at 3.6-angstrom resolution
Yan, C., Hang, J., Wan, R., Huang, M., Wong, C. C. L., & Shi, Y. (2015) · Science · doi:10.1126/science.aac7629 · Cited by 336
Single-Particle Imaging of Macromolecules by Cryo-Electron Microscopy
Frank, J. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134202 · Cited by 334
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Moore, S. D., & Sauer, R. T. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142733 · Cited by 328
The Eukaryotic Translation Initiation Factors eIF1 and eIF1A Induce an Open Conformation of the 40S Ribosome
Passmore, L. A., Schmeing, T. M., Maag, D., Applefield, D. J., Acker, M. G., Algire, M. A., Lorsch, J. R., & Ramakrishnan, V. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.03.018 · Cited by 327
The Anderson–Evans polyoxometalate: From inorganic building blocks via hybrid organic–inorganic structures to tomorrows “Bio-POM”
Blazevic, A., & Rompel, A. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.07.001 · Cited by 319
3.3 Å Cryo-EM Structure of a Nonenveloped Virus Reveals a Priming Mechanism for Cell Entry
Zhang, X., Jin, L., Fang, Q., Hui, W. H., & Zhou, Z. H. (2010) · Cell · doi:10.1016/j.cell.2010.03.041 · Cited by 322
Protein crystallography for non‐crystallographers, or how to get the best (but not more) from published macromolecular structures
Wlodawer, A., Minor, W., Dauter, Z., & Jaskólski, M. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06178.x · Cited by 334
Review of third and next generation synchrotron light sources
Bilderback, D. H., Elleaume, P., & Weckert, E. (2005) · Journal of Physics B Atomic Molecular and Optical Physics · doi:10.1088/0953-4075/38/9/022 · Cited by 309
Correlations between Shine-Dalgarno Sequences and Gene Features Such as Predicted Expression Levels and Operon Structures
Ma, J., Campbell, A., & Karlin, S. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.20.5733-5745.2002 · Cited by 308
Roles of Eukaryotic Ribosomal Proteins in Maturation and Transport of Pre-18S rRNA and Ribosome Function
Ferreira-Cerca, S., Pöll, G., Gleizes, P., Tschochner, H., & Milkereit, P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.005 · Cited by 330
Characteristics of the nuclear (18S, 5.8S, 28S and 5S) and mitochondrial (12S and 16S) rRNA genes of Apis mellifera (Insecta: Hymenoptera): structure, organization, and retrotransposable elements
Gillespie, J. J., Johnston, J. S., Cannone, J. J., & Gutell, R. R. (2006) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2006.00689.x · Cited by 302
Study of the Structural Dynamics of the E. coli 70S Ribosome Using Real-Space Refinement
Gao, H., Sengupta, J., Valle, M., Korostelev, A. A., Eswar, N., Stagg, S. M., Roey, P. V., Agrawal, R. K., Harvey, S. C., Šali, A., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00427-6 · Cited by 285
Antibiotic Resistance in Bacteria and Its Future for Novel Antibiotic Development
Hiroshi Yoneyama, C., & Katsumata, R. (2006) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70.1060 · Cited by 284
Global ribosome motions revealed with elastic network model
Wang, Y., Rader, A. J., Bahar, İ., & Jernigan, R. L. (2004) · Journal of Structural Biology · doi:10.1016/j.jsb.2004.01.005 · Cited by 284
Cryo-EM Visualization of a Viral Internal Ribosome Entry Site Bound to Human Ribosomes
Spahn, C. M. T., Jan, E., Mulder, A. M., Grassucci, R. A., Sarnow, P., & Frank, J. (2004) · Cell · doi:10.1016/j.cell.2004.08.001 · Cited by 266
Structural basis for messenger RNA movement on the ribosome
Yusupova, G. Z., Jenner, L. B., Rees, B., Moras, D., & Yusupov, M. (2006) · Nature · doi:10.1038/nature05281 · Cited by 264
Supramolecular assemblies of organo-functionalised hybrid polyoxometalates: from functional building blocks to hierarchical nanomaterials
Cameron, J. M., Guillemot, G., Galambos, T., Amin, S. S., Hampson, E., Haidaraly, K. M., Newton, G. N., & Izzet, G. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00832c · Cited by 264
A structural perspective on protein?protein interactions
Russell, R. B., Alber, F., Aloy, P., Davis, F. P., Korkin, D., Pichaud, M., Topf, M., & Šali, A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.04.006 · Cited by 267
The use of polyoxometalates in protein crystallography – An attempt to widen a well-known bottleneck
Bijelic, A., & Rompel, A. (2015) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2015.03.018 · Cited by 260
TectoRNA: modular assembly units for the construction of RNA nano-objects
Jaeger, L. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.2.455 · Cited by 255
Phylogenomics of Prokaryotic Ribosomal Proteins
Yutin, N., Puigbò, P., Koonin, E. V., & Wolf, Y. I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036972 · Cited by 273
Mg 2+ -dependent conformational change of RNA studied by fluorescence correlation and FRET on immobilized single molecules
Kim, H. D., Nienhaus, G. U., Ha, T., Orr, J. W., Williamson, J. R., & Chu, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.032077799 · Cited by 253
An assembly landscape for the 30S ribosomal subunit
Talkington, M. W. T., Siuzdak, G. E., & Williamson, J. R. (2005) · Nature · doi:10.1038/nature04261 · Cited by 256
RNA backbone: Consensus all-angle conformers and modular string nomenclature (an RNA Ontology Consortium contribution)
Richardson, J. S., Schneider, B., Murray, L. W., Kapral, G. J., Immormino, R. M., Headd, J. J., Richardson, D. C., Ham, D., Hershkovits, E., Williams, L. D., et al. (2008) · RNA · doi:10.1261/rna.657708 · Cited by 250
Structure and Dynamics of a Processive Brownian Motor: The Translating Ribosome
Frank, J., & Gonzalez, R. L. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060408-173330 · Cited by 255
The function and synthesis of ribosomes
Lafontaine, D. L. J., & Tollervey, D. W. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35080045 · Cited by 246
The Small Subunit of the Mammalian Mitochondrial Ribosome
Koc, E. C., Burkhart, W., Blackburn, K., Moseley, M. A., & Spremulli, L. L. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100727200 · Cited by 246
A universal mode of helix packing in RNA.
Doherty, E. A., Batey, R., Masquida, B., & Doudna, J. A. (2001) · Nature Structural Biology · doi:10.1038/86221 · Cited by 246
Structure of the 30S translation initiation complex
Simonetti, A., Marzi, S., Myasnikov, A. G., Fabbretti, A., Yusupov, M., Gualerzi, C. O., & Klaholz, B. P. (2008) · Nature · doi:10.1038/nature07192 · Cited by 235
ANTIBIOTICS TARGETING RIBOSOMES: Resistance, Selectivity, Synergism, and Cellular Regulation
Yonath, A. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133130 · Cited by 231
Self-citation
Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
Pisarev, A. V., KOLUPAEVA, V. G., Yusupov, M., Hellen, C. U. T., & Pestova, T. V. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.90 · Cited by 227
Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-Å resolution
Armache, J., Jarasch, A., Anger, A. M., Villa, E., Becker, T. A., Bhushan, S., Jossinet, F., Habeck, M., Dindar, G., Franckenberg, S., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009999107 · Cited by 226
Identification and Analysis of Over 2000 Ribosomal Protein Pseudogenes in the Human GenomePreprint
Zhang, Z., Harrison, P., & Gerstein, M. (2002) · Genome Research · doi:10.1101/gr.331902 · Cited by 219
Mechanisms of Streptomycin Resistance: Selection of Mutations in the 16S rRNA Gene Conferring Resistance
Springer, B., Kidan, Y. G., Prammananan, T., Ellrott, K., Böttger, E. C., & Sander, P. (2001) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.45.10.2877-2884.2001 · Cited by 207
RNA backbone is rotameric
Murray, L. J. W., Arendall, W. B., Richardson, D. C., & Richardson, J. S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1835769100 · Cited by 201
New roles for structure in biology and drug discovery.
Russell, R. B., & Eggleston, D. S. (2000) · Nature Structural Biology · doi:10.1038/80691 · Cited by 201
Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
Stark, H., Rodnina, M. V., Wieden, H., Zemlin, F., Wintermeyer, W., & van Heel, M. (2002) · Nature Structural Biology · doi:10.1038/nsb859 · Cited by 201
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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
Quantitative analysis of nucleic acid three-dimensional structures
Gendron, P., Lemieux, S., & Major, F. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4626 · Cited by 195
Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways
Whitford, P. C., Geggier, P., Altman, R. B., Blanchard, S. C., Onuchic, J. N., & Sanbonmatsu, K. Y. (2010) · RNA · doi:10.1261/rna.2035410 · Cited by 193
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Dallas, A., & Noller, H. F. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00356-2 · Cited by 192
Structure and Function of Noncanonical Nucleobases
Carell, T., Brandmayr, C., Hienzsch, A., Müller, M., Pearson, D., Reiter, V., Thoma, I., Thumbs, P., & Wagner, M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201193 · Cited by 200
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Peske, F., Savelsbergh, A., Katunin, V. I., Rodnina, M. V., & Wintermeyer, W. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.097 · Cited by 185
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Treiber, D. K., & Williamson, J. R. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00206-2 · Cited by 189
Fine-tuning of the ribosomal decoding center by conserved methyl-modifications in the Escherichia coli 16S rRNA
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Lomakin, I. B., & Steitz, T. A. (2013) · Nature · doi:10.1038/nature12355 · Cited by 189
Mass Measurements of Increased Accuracy Resolve Heterogeneous Populations of Intact Ribosomes
McKay, A. R., Ruotolo, B. T., Ilag, L. L., & Robinson, C. V. (2006) · Journal of the American Chemical Society · doi:10.1021/ja061468q · Cited by 177
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Yoshihama, M., Uechi, T., Asakawa, S., Kawasaki, K., Kato, S., Higa, S., Maeda, N., Minoshima, S., Tanaka, T., Shimizu, N., et al. (2002) · Genome Research · doi:10.1101/gr.214202 · Cited by 177

Authors: Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., & Yonath, A.
Affiliations: Weizmann Institute of Science (IL)
ORCID: Schluenzen, Frank
Zarivach, Raz
Bashan, Anat
Agmon, Ilana
Yonath, Ada
Venue: Cell
Publisher: Elsevier BV
Published: 2000-09
Volume: 102
Issue: 5
Pages: 615-623
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)00084-2
OpenAlex: W2092617311
Cited by: 979
References: 72
Citations by year: 2026: 11 · 2025: 13 · 2024: 18 · 2023: 28 · 2022: 18 · 2021: 26 · 2020: 27 · 2019: 18 · 2018: 22 · 2017: 25 · 2016: 18 · 2015: 31 · 2014: 26 · 2013: 27 · 2012: 43
FWCI: 28.84
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4702 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM-34360, R01GM034360)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: small ribosomal subunit, ribosome structure, Thermus thermophilus, decoding center, tRNA binding, mRNA translocation, translation fidelity, ribosomal proteins
MeSH terms: Binding Sites, Models, Molecular, Nucleic Acid Conformation, Protein Conformation, Ribosomes, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal, 16S, RNA, Transfer, Structure-Activity Relationship, Thermus thermophilus, Crystallography, X-Ray, Base Pairing

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Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

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