› 1qst

X-ray diffraction
1.7Å resolution

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5

Released:
DOI: 10.2210/pdb1qst/pdb
PDB entry 1qst coloured by chain, front view.
PDB entry 1qst coloured by chain, side view.
PDB entry 1qst coloured by chain, top view.
Source organism: Tetrahymena thermophila
Primary publication:
Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide.
Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R
Nature 401 93-8 (1999)
PMID: 10485713

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase GCN5 Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 19.13 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27198 (Residues: 49-208; Coverage: 38%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand EPE 1 x EPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2, NSLS BEAMLINE X8C
Spacegroup: P3221
Unit cell:
a: 64.1Å b: 64.1Å c: 97.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.278
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Histone acetyltransferases.
Roth et al. (2001)
37 more

6 mentions without citation

The hexosamine signaling pathway: O-GlcNAc cycling in feast or famine.
Hanover et al. (2010)
5 more