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. 2001 Apr 20;105(2):269-79.
doi: 10.1016/s0092-8674(01)00317-8.

Crystal structure of a SIR2 homolog-NAD complex

J Min  1 , J Landry, R Sternglanz, R M Xu
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Free article

Crystal structure of a SIR2 homolog-NAD complex

J Min et al. Cell. .
Free article

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 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.

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Comment in

  • Deciphering NAD-dependent deacetylases.
    Dutnall RN, Pillus L. Dutnall RN, et al. Cell. 2001 Apr 20;105(2):161-4. doi: 10.1016/s0092-8674(01)00305-1. Cell. 2001. PMID: 11336664 Review. No abstract available.

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