1ICI: Crystal Structure Of A Sir2 Homolog-nad Complex

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.
PDB ID: 1ICIDownload
MMDB ID: 16174
PDB Deposition Date: 2001/4/1
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 1ICI: dimeric; determined by author
Molecular Components in 1ICI
Label Count Molecule
Proteins (2 molecules)
Transcriptional Regulatory Protein, Sir2 Family(Gene symbol: AF_RS08430)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB