1j8f | pdb_00001j8f
HUMAN SIRT2 HISTONE DEACETYLASE
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Overview
Sir2 is an NAD-dependent histone deacetylase that mediates transcriptional, silencing at mating-type loci, telomeres and ribosomal gene clusters, and, has a critical role in the determination of life span in yeast and, Caenorhabditis elegans. The 1.7 A crystal structure of the 323 amino acid, catalytic core of human SIRT2, a homolog of yeast Sir2, reveals an, NAD-binding domain, which is a variant of the Rossmann fold, and a smaller, domain composed of a helical module and a zinc-binding module. A conserved, large groove at the interface of the two domains is the likely site of, catalysis based on mutagenesis. Intersecting this large groove, there is a, pocket formed by the helical module. The pocket is lined with hydrophobic, residues conserved within each of the five Sir2 classes, suggesting that, it is a class-specific protein-binding site.
About this Structure
1J8F is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the histone deacetylase SIRT2., Finnin MS, Donigian JR, Pavletich NP, Nat Struct Biol. 2001 Jul;8(7):621-5. PMID:11427894
Page seeded by OCA on Mon Nov 12 17:38:20 2007
