› 3to6

X-ray diffraction
2.1Å resolution

Crystal structure of yeast Esa1 HAT domain complexed with H4K16CoA bisubstrate inhibitor

Released:
DOI: 10.2210/pdb3to6/pdb
PDB entry 3to6 coloured by chain, front view.
PDB entry 3to6 coloured by chain, side view.
PDB entry 3to6 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
MYST protein acetyltransferase activity requires active site lysine autoacetylation.
Yuan H, Rossetto D, Mellert H, Dang W, Srinivasan M, Johnson J, Hodawadekar S, Ding EC, Speicher K, Abshiru N, Perry R, Wu J, Yang C, Zheng YG, Speicher DW, Thibault P, Verreault A, Johnson FB, Berger SL, Sternglanz R, McMahon SB, Côté J, Marmorstein R
EMBO J 31 58-70 (2012)
PMID: 22020126

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-135465 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone acetyltransferase ESA1 Chain: A
Molecule details ›
Chain: A
Length: 276 amino acids
Theoretical weight: 33.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08649 (Residues: 160-435; Coverage: 62%)
Gene names: ESA1, O5257, YOR244W
Sequence domains:
Structure domains:
Histone H4 Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.33 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
UniProt:
  • Canonical: P02309 (Residues: 12-23; Coverage: 12%)
Gene names: HHF1, HHF2, N2752, YBR009C, YBR0122, YNL030W

Ligands and Environments


Cofactor: Ligand CMC 1 x CMC
No bound ligands
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: I4132
Unit cell:
a: 183.282Å b: 183.282Å c: 183.282Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.232
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

22 review citations

The growing landscape of lysine acetylation links metabolism and cell signalling.
Choudhary et al. (2014)
21 more

5 mentions without citation

Writers and readers of histone acetylation: structure, mechanism, and inhibition.
Marmorstein et al. (2014)
4 more