1ici
From Proteopedia
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CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX
Overview
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.
About this Structure
1ICI is a Single protein structure of sequence from Archaeoglobus fulgidus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of a SIR2 homolog-NAD complex., Min J, Landry J, Sternglanz R, Xu RM, Cell. 2001 Apr 20;105(2):269-79. PMID:11336676
Page seeded by OCA on Thu Feb 21 13:10:21 2008
