› 4hkf

X-ray diffraction
1.7Å resolution

Crystal structure of Danio rerio MEC-17 catalytic domain in complex with acetyl-CoA

Released:
DOI: 10.2210/pdb4hkf/pdb
PDB entry 4hkf coloured by chain, front view.
PDB entry 4hkf coloured by chain, side view.
PDB entry 4hkf coloured by chain, top view.
Source organism: Danio rerio
Primary publication:
Molecular basis of the acetyltransferase activity of MEC-17 towards α-tubulin.
Li W, Zhong C, Li L, Sun B, Wang W, Xu S, Zhang T, Wang C, Bao L, Ding J
Cell Res 22 1707-11 (2012)
PMID: 23128673

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tubulin N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.6 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6PH17 (Residues: 1-188; Coverage: 63%)
Gene names: atat1, mec17, si:ch211-152p11.5, zgc:65893
Sequence domains: GNAT acetyltransferase, Mec-17
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 57.627Å b: 65.874Å c: 104.674Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.145 0.192
Expression system: Escherichia coli

Quick links

Citations

3 review citations

ChSeq: A database of chameleon sequences.
Li et al. (2015)
2 more

1 mention without citation

Molecular basis of the acetyltransferase activity of MEC-17 towards α-tubulin.
Li et al. (2012)