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http://purl.uniprot.org/citations/12185246http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12185246http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12185246http://www.w3.org/2000/01/rdf-schema#comment"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-A 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 bound identically by either the A or P loop of the 23S rRNA. Combining the separate P and A site substrate complexes into one model reveals interactions that may occur when both are present simultaneously. The alpha-NH(2) group of an aminoacylated fragment in the A site forms one hydrogen bond with the N3 of A2486 (2451) and may form a second hydrogen bond either with the 2' OH of the A-76 ribose in the P site or with the 2' OH of A2486 (2451). These interactions position the alpha amino group adjacent to the carbonyl carbon of esterified P site substrate in an orientation suitable for a nucleophilic attack."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.org/dc/terms/identifier"doi:10.1073/pnas.172404099"xsd:string
http://purl.uniprot.org/citations/12185246http://purl.org/dc/terms/identifier"doi:10.1073/pnas.172404099"xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Steitz T.A."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Steitz T.A."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Hansen J.L."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Hansen J.L."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Moore P.B."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Moore P.B."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Schmeing T.M."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/author"Schmeing T.M."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/pages"11670-11675"xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/pages"11670-11675"xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/title"Structural insights into peptide bond formation."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/title"Structural insights into peptide bond formation."xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/12185246http://purl.uniprot.org/core/volume"99"xsd:string
http://purl.uniprot.org/citations/12185246http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12185246
http://purl.uniprot.org/citations/12185246http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12185246