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| pubmed-article:12535524 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12535524 | pubmed:dateCreated | 2003-1-21 | lld:pubmed |
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| pubmed-article:12535524 | pubmed:abstractText | Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3' end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism. | lld:pubmed |
| pubmed-article:12535524 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12535524 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12535524 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12535524 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12535524 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12535524 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:12535524 | pubmed:author | pubmed-author:ZarivachRazR | lld:pubmed |
| pubmed-article:12535524 | pubmed:author | pubmed-author:BerisioRitaR | lld:pubmed |
| pubmed-article:12535524 | pubmed:author | pubmed-author:YonathAdaA | lld:pubmed |
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| pubmed-article:12535524 | pubmed:author | pubmed-author:AgmonIlanaI | lld:pubmed |
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| pubmed-article:12535524 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12535524 | pubmed:volume | 11 | lld:pubmed |
| pubmed-article:12535524 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12535524 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12535524 | pubmed:pagination | 91-102 | lld:pubmed |
| pubmed-article:12535524 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:12535524 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12535524 | pubmed:articleTitle | Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression. | lld:pubmed |
| pubmed-article:12535524 | pubmed:affiliation | Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel. | lld:pubmed |
| pubmed-article:12535524 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12535524 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12535524 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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