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Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution
Open accessAbstract
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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“These changes could be mediated by S12, which is in close proximity to the top of h44 (43, 58) and also appears to interact with Tet(O) (45).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [43]
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Cites
[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
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
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Razi, A., Britton, R. A., & Ortega, J. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw1231 · Cited by 27
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Morosyuk, S. V., SantaLucia, J., & Cunningham, P. R. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4432 · Cited by 22
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Polacek, N., Swaney, S. M., Shinabarger, D. L., & Mankin, A. S. (2002) · Biochemistry · doi:10.1021/bi026040s · Cited by 22
Guillier, M., Allemand, F., Graffe, M., Raibaud, S., Dardel, F., Springer, M., & Chiaruttini, C. (2005) · RNA · doi:10.1261/rna.7134305 · Cited by 22
Xu, J. J., Zhang, J. Z. H., & Xiang, Y. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3076605 · Cited by 21
Metadata
- 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)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 102
- Issue
- 5
- Pages
- 615-623
- ISSN
- 0092-8674 (ISSN-L)
- 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
- 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
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 ›
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