Title : Structure and chemistry of the Sir2 family of NAD+-dependent histone/protein deactylases.

Pub. Date : 2004 Dec

PMID : 15506920






2 Functional Relationships(s)
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1 We have determined the X-ray crystal structure of a Sir2 homologue from yeast Hst2 (yHst2), in various liganded forms, including the yHst2/acetyl-Lys-16 histone H4/NAD(+) ternary complex; we have also performed related biochemical studies to address the conserved mode of catalysis by these enzymes as well as the distinguishing features that allow different members of the family to target their respective cognate substrates. NAD histone deacetylase HST2 Saccharomyces cerevisiae S288C
2 We have determined the X-ray crystal structure of a Sir2 homologue from yeast Hst2 (yHst2), in various liganded forms, including the yHst2/acetyl-Lys-16 histone H4/NAD(+) ternary complex; we have also performed related biochemical studies to address the conserved mode of catalysis by these enzymes as well as the distinguishing features that allow different members of the family to target their respective cognate substrates. NAD histone deacetylase HST2 Saccharomyces cerevisiae S288C