The DOI matches its Crossref record.
Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
Open accessAbstract
During protein synthesis, elongation factor G (EF-G) binds to the ribosome and promotes the step of translocation, a process in which tRNA moves from the A to the P site of the ribosome and the mRNA is advanced by one codon. By using three-dimensional cryo-electron microscopy, we have visualized EF-G in a ribosome–EF-G–GDP–fusidic acid complex. Fitting the crystal structure of EF-G–GDP into the cryo density map reveals a large conformational change mainly associated with domain IV, the domain that mimics the shape of the anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA Phe , EF-Tu, and a GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, whose position in the ribosome is known from a study of the pretranslocational complex, implying that EF-G displaces the A-site tRNA to the P site by physical interaction with the anticodon arm.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
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
Self-citationThe 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
The A-Z of bacterial translation inhibitors
Wilson, D. N. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409230903307311 · Cited by 322
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
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
Self-citationRole of Domains 4 and 5 in Elongation Factor G Functions on the Ribosome
Savelsbergh, A., Matassova, N. B., Rodnina, M. V., & Wintermeyer, W. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3886 · Cited by 115
Cameron, D. M., Thompson, J., March, P. E., & Dahlberg, A. E. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00235-8 · Cited by 99
Spahn, C. M. T., Blaha, G., Agrawal, R. K., Penczek, P., Grassucci, R. A., Trieber, C. A., Connell, S. R., Taylor, D. E., Nierhaus, K. H., & Frank, J. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00238-6 · Cited by 81
Self-citationRibosomal proteins: Structure, function, and evolution
Korobeinikova, A. V., Garber, M. B., & Gongadze, G. M. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060028 · Cited by 63
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
Self-citationDomain IV of elongation factor G from Thermus thermophilus is strictly required for translocation
Martemyanov, K. A., & Gudkov, A. T. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00635-3 · Cited by 34
Chimeras of bacterial translation factors Tet(O) and EF‐G
Thakor, N. S., Nechifor, R., Scott, P. G., Keelan, M., Taylor, D. E., & Wilson, K. S. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.023 · Cited by 4
Metadata
- Authors
- Agrawal, R. K., Penczek, P., Grassucci, R. A., & Frank, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-05-26
- Volume
- 95
- Issue
- 11
- Pages
- 6134-6138
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2152348402
- Cited by
- 325
- References
- 0
- FWCI
- 11.59
- Type
- journal article
- Language
- en
- Open access
- green
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.