| http://purl.uniprot.org/citations/16306996 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/16306996 | http://www.w3.org/2000/01/rdf-schema#comment | "The large ribosomal subunit catalyses the reaction between the alpha-amino group of the aminoacyl-tRNA bound to the A site and the ester carbon of the peptidyl-tRNA bound to the P site, while preventing the nucleophilic attack of water on the ester, which would lead to unprogrammed deacylation of the peptidyl-tRNA. Here we describe three new structures of the large ribosomal subunit of Haloarcula marismortui (Hma) complexed with peptidyl transferase substrate analogues that reveal an induced-fit mechanism in which substrates and active-site residues reposition to allow the peptidyl transferase reaction. Proper binding of an aminoacyl-tRNA analogue to the A site induces specific movements of 23S rRNA nucleotides 2618-2620 (Escherichia coli numbering 2583-2585) and 2541(2506), thereby reorienting the ester group of the peptidyl-tRNA and making it accessible for attack. In the absence of the appropriate A-site substrate, the peptidyl transferase centre positions the ester link of the peptidyl-tRNA in a conformation that precludes the catalysed nucleophilic attack by water. Protein release factors may also function, in part, by inducing an active-site rearrangement similar to that produced by the A-site aminoacyl-tRNA, allowing the carbonyl group and water to be positioned for hydrolysis."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature04152"xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/author | "Steitz T.A."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/author | "Strobel S.A."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/author | "Schmeing T.M."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/author | "Huang K.S."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/pages | "520-524"xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/title | "An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA."xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://purl.uniprot.org/core/volume | "438"xsd:string |
| http://purl.uniprot.org/citations/16306996 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/16306996 |
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| http://purl.uniprot.org/uniprot/#_P18138-mappedCitation-16306996 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/16306996 |
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