1ICI

CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD COMPLEX

Summary for 1ICI

• Entry DOI: 10.2210/pdb1ici/pdb
• Descriptor: TRANSCRIPTIONAL REGULATORY PROTEIN, SIR2 FAMILY, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: rossmann fold, zinc ribbon, protein deacetylase, nad-binding, transcription
• Biological source: Archaeoglobus fulgidus
• Cellular location: Cytoplasm : O28597
• Total number of polymer chains: 2
• Total formula weight: 58331.06

Authors

Min, J.,Landry, J.,Sternglanz, R.,Xu, R.-M. (deposition date: 2001-04-01, release date: 2001-05-02, Last modification date: 2024-02-07)

Primary citation

Min, J.,Landry, J.,Sternglanz, R.,Xu, R.M.
Crystal structure of a SIR2 homolog-NAD complex.
Cell(Cambridge,Mass.), 105:269-279, 2001

PubMed 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.

PubMed: 11336676
DOI: 10.1016/S0092-8674(01)00317-8

Experimental method

X-RAY DIFFRACTION (2.1 Å)