1q1a
From Proteopedia
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Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Overview
Sir2 proteins are NAD(+)-dependant protein deactylases that have been, implicated in playing roles in gene silencing, DNA repair, genome, stability, longevity, metabolism, and cell physiology. To define the, mechanism of Sir2 activity, we report the 1.5 A crystal structure of the, yeast Hst2 (yHst2) Sir2 protein in ternary complex with 2'-O-acetyl ADP, ribose and an acetylated histone H4 peptide. The structure captures both, ligands meeting within an enclosed tunnel between the small and large, domains of the catalytic protein core and permits the assignment of a, detailed catalytic mechanism for the Sir2 proteins that is consistent with, solution and enzymatic studies. Comparison of the ternary complex with the, yHst2/NAD(+) complex, also reported here, and nascent yHst2 structure also, reveals that NAD(+) binding accompanies intramolecular loop rearrangement, for more stable NAD(+) and acetyl-lysine binding, and that acetyl-lysine, peptide binding induces a trimer-monomer protein transition involving, nonconserved Sir2 residues.
About this Structure
1Q1A is a Protein complex structure of sequences from Saccharomyces cerevisiae with ZN and OAD as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide., Zhao K, Chai X, Marmorstein R, Structure. 2003 Nov;11(11):1403-11. PMID:14604530
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