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http://purl.uniprot.org/citations/9187657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9187657http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9187657http://www.w3.org/2000/01/rdf-schema#comment"The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.org/dc/terms/identifier"doi:10.1038/nsb0697-483"xsd:string
http://purl.uniprot.org/citations/9187657http://purl.org/dc/terms/identifier"doi:10.1038/nsb0697-483"xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Petros A.M."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Petros A.M."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Yu L."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Yu L."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Zhong P."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Zhong P."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Walter K."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Walter K."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Fesik S.W."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Fesik S.W."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Schnuchel A."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Schnuchel A."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Holzman T.F."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Holzman T.F."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Severin J.M."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/author"Severin J.M."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/9187657http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string