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http://purl.uniprot.org/citations/11336676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11336676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11336676http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/11336676http://www.w3.org/2000/01/rdf-schema#comment"The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 A and 2.4 A resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAD-dependent protein deacetylation by this family of enzymes."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(01)00317-8"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.org/dc/terms/identifier"doi:10.1016/s0092-8674(01)00317-8"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Min J."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Landry J."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Landry J."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Sternglanz R."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Sternglanz R."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Xu R.-M."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/author"Xu R.-M."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/pages"269-279"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/pages"269-279"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/title"Crystal structure of a SIR2 homolog-NAD complex."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/title"Crystal structure of a SIR2 homolog-NAD complex."xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/11336676http://purl.uniprot.org/core/volume"105"xsd:string
http://purl.uniprot.org/citations/11336676http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11336676