1J8F

Structure of the histone deacetylase SIRT2.

(2001) Nat Struct Biol 8: 621-625

• PubMed: 11427894 Search on PubMed
• DOI: https://doi.org/10.1038/89668
• Primary Citation of Related Structures:  
  1J8F


• 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.

   View More

---

Organizational Affiliation: 

Cellular Biochemistry and Biophysics Program, and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.