http://purl.uniprot.org/citations/11336676 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11336676 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/11336676 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
http://purl.uniprot.org/citations/11336676 | http://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/11336676 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(01)00317-8"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0092-8674(01)00317-8"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Min J."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Min J."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Landry J."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Landry J."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Sternglanz R."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Sternglanz R."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Xu R.-M."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/author | "Xu R.-M."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/name | "Cell"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/pages | "269-279"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/pages | "269-279"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/title | "Crystal structure of a SIR2 homolog-NAD complex."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/title | "Crystal structure of a SIR2 homolog-NAD complex."xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/volume | "105"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://purl.uniprot.org/core/volume | "105"xsd:string |
http://purl.uniprot.org/citations/11336676 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11336676 |