Crystal structure of a SIR2 homolog-NAD complex

Min, J. R., Landry, J., Sternglanz, R., Xu, R. M. (April 2001) Crystal structure of a SIR2 homolog-NAD complex. Cell, 105 (2). pp. 269-279. ISSN 0092-8674

URL: http://www.ncbi.nlm.nih.gov/pubmed/11336676

DOI: 10.1016/S0092-8674(01)00317-8

Abstract

The SIR2 protein family comprises a novel class of nicotinamide-adenine dinucleotide (NAD)-dependent protein deacetylases that function in transcriptional silencing, DNA repair, and life-span extension in Saccharomyces cerevisiae. Two crystal structures of a SIR2 homolog from Archaeoglobus fulgidus complexed with NAD have been determined at 2.1 Angstrom and 2.4 Angstrom resolutions. The structures reveal that the protein consists of a large domain having a Rossmann fold and a small domain containing a three-stranded zinc ribbon motif. NAD is bound in a pocket between the two domains. A distinct mode of NAD binding and an unusual configuration of the zinc ribbon motif are observed. The structures also provide important insights into the catalytic mechanism of NAB-dependent protein deacetylation by this family of enzymes.

Item Type:	Paper
Uncontrolled Keywords:	SILENCING PROTEIN SIR2 SACCHAROMYCES-CEREVISIAE TELOMERIC HETEROCHROMATIN DEACETYLASE ACTIVITY HISTONE DEACETYLASE SIR2-LIKE PROTEINS DIFFRACTION DATA GENE-EXPRESSION ZINC RIBBON YEAST
Subjects:	bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein characterization bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering Investigative techniques and equipment > x ray crystallography
CSHL Authors:	Min, Jinrong Xu, Rui-Ming
Communities:	CSHL labs > Xu lab
Depositing User:	Matt Covey
Date:	April 2001
Date Deposited:	17 Jan 2014 20:01
Last Modified:	17 Jan 2014 20:01
Related URLs:	Publisher
URI:	https://repository.cshl.edu/id/eprint/29273

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