1J8F

HUMAN SIRT2 HISTONE DEACETYLASE

Summary for 1J8F

• Entry DOI: 10.2210/pdb1j8f/pdb
• Descriptor: SIRTUIN 2, ISOFORM 1, ZINC ION (3 entities in total)
• Functional Keywords: sirt2, gene regulation, transferase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 109792.34

Authors

Pavletich, N.P.,Finnin, M.S.,Donigian, J.R. (deposition date: 2001-05-21, release date: 2001-07-06, Last modification date: 2024-10-30)

Primary citation

Finnin, M.S.,Donigian, J.R.,Pavletich, N.P.
Structure of the histone deacetylase SIRT2.
Nat.Struct.Biol., 8:621-625, 2001

PubMed Abstract: 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.

PubMed: 11427894
DOI: 10.1038/89668

Experimental method

X-RAY DIFFRACTION (1.7 Å)