› 2h2i

X-ray diffraction
1.8Å resolution

The Structural basis of Sirtuin Substrate Affinity

Released:
DOI: 10.2210/pdb2h2i/pdb
PDB entry 2h2i coloured by chain, front view.
PDB entry 2h2i coloured by chain, side view.
PDB entry 2h2i coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The structural basis of sirtuin substrate affinity.
Cosgrove MS, Bever K, Avalos JL, Muhammad S, Zhang X, Wolberger C
Biochemistry 45 7511-21 (2006)
PMID: 16768447

Function and Biology Details

Reaction catalysed: 
(1a) [protein]-N(6)-acetyl-L-lysine + NAD(+) = [protein]-N(6)-(1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl)-L-lysine + nicotinamide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD-dependent protein deacetylase Chain: A
Molecule details ›
Chain: A
Length: 246 amino acids
Theoretical weight: 27.57 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYW0 (Residues: 1-246; Coverage: 100%)
Gene names: TM_0490, cobB, sir2
Sequence domains: Sir2 family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand ZPG 1 x ZPG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P432
Unit cell:
a: 133.107Å b: 133.107Å c: 133.107Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.03 0.186 0.213
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Protein binding specificity versus promiscuity.
Schreiber et al. (2011)
16 more

2 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
1 more