期刊
CELL
卷 105, 期 2, 页码 269-279出版社
CELL PRESS
DOI: 10.1016/S0092-8674(01)00317-8
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资金
- NIGMS NIH HHS [GM55641] Funding Source: Medline
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 Angstrom and 2.4 Angstrom 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 NAB-dependent protein deacetylation by this family of enzymes.
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