Crystal structure of a SIR2 homolog-NAD complex

Min, J. R., Landry, J., Sternglanz, R., Xu, R. M. (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:
Communities: CSHL labs > Xu lab
Depositing User: Matt Covey
Date Deposited: 17 Jan 2014 20:01
Last Modified: 17 Jan 2014 20:01
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29273

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving