1ici
From Proteopedia
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'''CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX''' | '''CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX''' | ||
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[[Category: Sternglanz, R.]] | [[Category: Sternglanz, R.]] | ||
[[Category: Xu, R M.]] | [[Category: Xu, R M.]] | ||
| - | [[Category: | + | [[Category: Nad-binding]] |
| - | [[Category: | + | [[Category: Protein deacetylase]] |
| - | [[Category: | + | [[Category: Rossmann fold]] |
| - | [[Category: | + | [[Category: Zinc ribbon]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:50:42 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 16:50, 2 May 2008
CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX
Overview
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 A and 2.4 A 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 NAD-dependent protein deacetylation by this family of enzymes.
About this Structure
1ICI is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a SIR2 homolog-NAD complex., Min J, Landry J, Sternglanz R, Xu RM, Cell. 2001 Apr 20;105(2):269-79. PMID:11336676 Page seeded by OCA on Fri May 2 19:50:42 2008
