The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Insights into substrate stabilization from snapshots of the peptidyl transferase center of the intact 70S ribosome
Open accessAbstract
Protein synthesis is catalyzed in the peptidyl transferase center (PTC), located in the large (50S) subunit of the ribosome. No high-resolution structure of the intact ribosome has contained a complete active site including both A- and P-site tRNAs. In addition, although past structures of the 50S subunit have found no ordered proteins at the PTC, biochemical evidence suggests that specific proteins are capable of interacting with the 3′ ends of tRNA ligands. Here we present structures, at 3.6-Å and 3.5-Å resolution respectively, of the 70S ribosome in complex with A- and P-site tRNAs that mimic pre- and post-peptidyl-transfer states. These structures demonstrate that the PTC is very similar between the 50S subunit and the intact ribosome. They also reveal interactions between the ribosomal proteins L16 and L27 and the tRNA substrates, helping to elucidate the role of these proteins in peptidyl transfer.
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Citations
Cites
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
Cited by
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
Self-citationRevisiting the structures of several antibiotics bound to the bacterial ribosome
Bulkley, D., Innis, C. A., Blaha, G., & Steitz, T. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008685107 · Cited by 308
Protein synthesis by ribosomes with tethered subunits
Orelle, C., Carlson, E. D., Szal, T., Florin, T., Jewett, M. C., & Mankin, A. S. (2015) · Nature · doi:10.1038/nature14862 · Cited by 231
Jenner, L., Starosta, A. L., Terry, D. S., Mikolajka, A., Filonava, L., Yusupov, M., Blanchard, S. C., Wilson, D. N., & Yusupova, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216691110 · Cited by 204
Structural and functional insights into the mode of action of a universally conserved Obg GTPase.
Feng, B., Mandava, C. S., Guo, Q., Wang, J., Cao, W., Li, N., Zhang, Y., Zhang, Y., Wang, Z., Wu, J., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001866 · Cited by 129
Metadata
- Authors
- Voorhees, R. M., Weixlbaumer, A., Loakes, D., Kelley, A. C., & Ramakrishnan, V
- Venue
- Nature Structural & Molecular Biology
- Published
- 2009-04-12
- Volume
- 16
- Issue
- 5
- Pages
- 528-533
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2152425069
- Cited by
- 371
- References
- 1
- FWCI
- 14.64
- Type
- journal article
- Language
- en
- Open access
- green
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