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http://purl.uniprot.org/citations/12372303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12372303http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12372303http://www.w3.org/2000/01/rdf-schema#comment"Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of Rubisco large subunit methyltransferase in a pseudo-bisubstrate complex with S-adenosylhomocysteine and a HEPES ion reveals an all-beta architecture for the SET domain embedded within a larger alpha-helical enzyme fold. Conserved regions of the SET domain bind S-adenosylmethionine and substrate lysine at two sites connected by a pore. We propose that methyl transfer is catalyzed by a conserved Tyr at a narrow pore connecting the sites. The cofactor enters by a "back door" on the opposite side of the enzyme from substrate, promoting highly specific protein recognition and allowing addition of multiple methyl groups."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01000-0"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(02)01000-0"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Hurley J.H."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Trievel R.C."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Trievel R.C."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Dirk L.M."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Dirk L.M."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Houtz R.L."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Houtz R.L."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Beach B.M."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/author"Beach B.M."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/pages"91-103"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/pages"91-103"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/title"Structure and catalytic mechanism of a SET domain protein methyltransferase."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/title"Structure and catalytic mechanism of a SET domain protein methyltransferase."xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/volume"111"xsd:string
http://purl.uniprot.org/citations/12372303http://purl.uniprot.org/core/volume"111"xsd:string