2002
DOI: 10.1073/pnas.172404099
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Structural insights into peptide bond formation

Abstract: The large ribosomal subunit catalyzes peptide bond formation and will do so by using small aminoacyl-and peptidyl-RNA fragments of tRNA. We have refined at 3-Å resolution the structures of both A and P site substrate and product analogues, as well as an intermediate analogue, bound to the Haloarcula marismortui 50S ribosomal subunit. A P site substrate, CCA-Phe-caproic acid-biotin, binds equally to both sites, but in the presence of sparsomycin binds only to the P site. The CCA portions of these analogues are … Show more

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Cited by 269 publications
(276 citation statements)
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“…The program started with the observation that linezolid and sparsomycin ( 6 , a non‐selective antibiotic) had overlapping binding sites within the peptidyl transferase center of the 50S ribosomal unit (Figure 7). 42, 43 …”
Section: Protein Synthesis Inhibitorsmentioning
confidence: 99%
“…The program started with the observation that linezolid and sparsomycin ( 6 , a non‐selective antibiotic) had overlapping binding sites within the peptidyl transferase center of the 50S ribosomal unit (Figure 7). 42, 43 …”
Section: Protein Synthesis Inhibitorsmentioning
confidence: 99%
“…As such, it is a major participant in the remote interactions that govern the accurate positioning of the tRNA substrates. 8,9,41 The crucial contribution of H69 interactions to productive alignment of the A-site tRNA substrate is demonstrated by the finding that in their absence similar, albeit distinctly different, binding modes were observed within the PTC, [39][40][41] all requiring conformational rearrangements in order to participate in peptide bond formation. 10 Lack of remote interactions could be due to the disorder of H69, as observed in the H50S high-resolution structure, 2,3 or result from the use of tRNA analogues that are too short to reach the upper rim of the PTC cavity, where the components providing the remote interactions reside.…”
Section: Regulation Discrimination and Signaling Subunit Associationmentioning
confidence: 99%
“…10 Lack of remote interactions could be due to the disorder of H69, as observed in the H50S high-resolution structure, 2,3 or result from the use of tRNA analogues that are too short to reach the upper rim of the PTC cavity, where the components providing the remote interactions reside. 39,40 The structures of the substrates bound ribosome 6 and to the large subunit, D50S, 8 indicate that similar to Helix H69, protein L16 is also involved in moderating accurate substrate positioning. This protein is located at the upper rim periphery of the PTC cavity [Plate 1(c)], in a position allowing interactions with the acceptor stem of the A-site tRNA, and these remote interactions appear to be of major importance.…”
Section: Regulation Discrimination and Signaling Subunit Associationmentioning
confidence: 99%
“…R ecent discoveries have shown that RNA plays a larger role in biology than previously realized, e.g., in posttranscriptional regulation (1), development (2,3), immunity (4,5), and peptide bond formation (6,7). It is necessary to determine the native structures of RNAs to understand their mechanisms of action, and determining secondary structure is a crucial step in this process.…”
mentioning
confidence: 99%