1Q14

Structure and autoregulation of the yeast Hst2 homolog of Sir2

Summary for 1Q14

• Entry DOI: 10.2210/pdb1q14/pdb
• Descriptor: HST2 protein, ZINC ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: histone deacetylase, hydrolase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus (Potential): P53686
• Total number of polymer chains: 1
• Total formula weight: 40479.53

Authors

Zhao, K.,Chai, X.,Clements, A.,Marmorstein, R. (deposition date: 2003-07-18, release date: 2003-09-30, Last modification date: 2024-02-14)

Primary citation

Zhao, K.,Chai, X.,Clements, A.,Marmorstein, R.
Structure and autoregulation of the Yeast Hst2 homolog of Sir2
Nat.Struct.Biol., 10:864-871, 2003

PubMed Abstract: Yeast Hst2 (yHst2) is a member of the silencing information regulator 2 (Sir2) family of NAD(+)-dependent protein deacetylases that are implicated in transcriptional silencing, DNA repair, genome stability and longevity. The X-ray crystal structure of the full-length yHst2 protein reveals a central catalytic core domain fold that is characteristic of the other Sir2 homologs, and C- and N-terminal extensions that interact with the NAD(+) and acetyl-lysine substrate-binding sites, respectively, suggesting an autoregulatory function for these domains. Moreover, the N-terminal extension mediates formation of a homotrimer within the crystal lattice. Enzymatic and sedimentation equilibrium studies using deletion constructs of yHst2 support the involvement of the N- and C-terminal yHst2 regions and trimer formation in catalysis by yHst2. Together, these studies indicate that the sequence-divergent N- and C-terminal regions of the eukaryotic Sir2 proteins may have a particularly important role in their distinct substrate-binding properties, biological activities or both.

PubMed: 14502267
DOI: 10.1038/nsb978

Experimental method

X-RAY DIFFRACTION (2.5 Å)