› 3toa

X-ray diffraction
3Å resolution

Human MOF crystal structure with active site lysine partially acetylated

Released:
DOI: 10.2210/pdb3toa/pdb
PDB entry 3toa coloured by chain, front view.
PDB entry 3toa coloured by chain, side view.
PDB entry 3toa coloured by chain, top view.
Source organism: Homo sapiens
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190669 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase KAT8 Chain: A
Molecule details ›
Chain: A
Length: 303 amino acids
Theoretical weight: 35.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7Z6 (Residues: 177-458; Coverage: 62%)
Gene names: KAT8, MOF, MYST1, PP7073
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand CL 2 x CL
Ligand EDO 2 x EDO
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 46.255Å b: 58.534Å c: 121.501Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.246 0.265
Expression system: Escherichia coli

Quick links

Citations

24 review citations

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

5 mentions without citation

Histone acetyltransferases: challenges in targeting bi-substrate enzymes.
Wapenaar et al. (2016)
4 more