Structure of the Yeast Hst2 Protein Deacetylase in Ternary Complex with 2′-O-Acetyl ADP Ribose and Histone Peptide

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 Å crystal structure of the yeast Hst2 (yHst2) Sir2...

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Veröffentlicht in:	Structure (London) 2003-11, Vol.11 (11), p.1403-1411
Hauptverfasser:	Zhao, Kehao, Chai, Xiaomei, Marmorstein, Ronen
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Catalysis Catalytic Domain Crystallography, X-Ray deactylase deactylases DNA Repair Histones - chemistry Hst2 protein Lysine - chemistry Models, Chemical Models, Molecular Molecular Sequence Data Peptides - chemistry Protein Binding Protein Conformation Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - physiology Sir2 protein Sirtuin 2 Sirtuins - chemistry Sirtuins - physiology Substrate Specificity
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