› 1qsn

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND COENZYME A AND HISTONE H3 PEPTIDE

Released:
DOI: 10.2210/pdb1qsn/pdb
PDB entry 1qsn coloured by chain, front view.
PDB entry 1qsn coloured by chain, side view.
PDB entry 1qsn coloured by chain, top view.
Source organisms:
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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158415 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase GCN5 Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 19.34 KDa
Source organism: Tetrahymena thermophila
Expression system: Escherichia coli
UniProt:
  • Canonical: Q27198 (Residues: 49-209; Coverage: 39%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase
Histone H3 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.16 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P61830 (Residues: 10-20; Coverage: 8%)
Gene names: HHT1, HHT2, N2749, SIN2, YBR010W, YBR0201, YNL031C

Ligands and Environments


Cofactor: Ligand COA 1 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P3221
Unit cell:
a: 65.09Å b: 65.09Å c: 96.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.239 0.266
Expression system: Escherichia coli

Quick links

Citations

35 review citations

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

21 mentions without citation

Acylation of Biomolecules in Prokaryotes: a Widespread Strategy for the Control of Biological Function and Metabolic Stress.
Hentchel et al. (2015)
20 more