The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA
Open accessAbstract
Ribosomes Caught in Translation: To synthesize proteins, the ribosome must select cognate transfer RNAs (tRNAs) based on base-pairing with the messenger RNA (mRNA) template (a process known as decoding), form a peptide bond, and then move the mRNA:tRNA assembly relative to the ribosome (a process known as translocation). Decoding and translocation require protein guanosine triphosphatases (GTPases), and, while high-resolution structures of the ribosome have greatly furthered our understanding of ribosome function, the detailed mechanism of these GTPases during the elongation cycle remains unclear. Two Research Articles now give a clearer view of these steps in bacterial protein synthesis (see the Perspective by Liljas ). Schmeing et al. (p. 688 , published online 15 October) present the crystal structure of the ribosome bound to Elongation factor-Tu (EF-Tu) and amino-acyl tRNA that gives insight into how EF-Tu contributes to accurate decoding. Gao et al. (p. 694 , published online 15 October) describe the crystal structure of the ribosome bound to Elongation factor-G (EF-G) trapped in a posttranslocation state by the antibiotic fusidic acid that gives insight into how EF-G functions in translocation.
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Cites
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Xia, T., SantaLucia, J., Burkard, M. E., Kierzek, R., Schroeder, S. J., Jiao, X., Cox, C., & Turner, D. H. (1998) · Biochemistry · doi:10.1021/bi9809425 · Cited by 1,140
Cited by
The Mechanism for Activation of GTP Hydrolysis on the Ribosome
Voorhees, R. M., Schmeing, T. M., Kelley, A. C., & Ramakrishnan, V. (2010) · Science · doi:10.1126/science.1194460 · Cited by 366
Self-citationCrystal 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
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
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
Ribosomal oxygenases are structurally conserved from prokaryotes to humans
Chowdhury, R., Sekirnik, R., Brissett, N. C., Krojer, T., Ho, C.-H., Ng, S. S., Clifton, I. J., Ge, W., Kershaw, N. J., Fox, G. C., et al. (2014) · Nature · doi:10.1038/nature13263 · Cited by 105
Metadata
- Authors
- Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y.-G., Murphy, F. V., Weir, J. R., & Ramakrishnan, V.
- Venue
- Science
- Published
- 2009-10-30
- Volume
- 326
- Issue
- 5953
- Pages
- 688-694
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2142672816
- Cited by
- 546
- References
- 2
- FWCI
- 20.16
- Type
- journal article
- Language
- en
- Open access
- green
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- Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y.-G., Murphy, F. V., Weir, J. R., & Ramakrishnan, V. (2009). The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA. Science. https://doi.org/10.1126/science.1179700
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