› 4if5

X-ray diffraction
1.7Å resolution

Structure of human Mec17

Released:
DOI: 10.2210/pdb4if5/pdb
PDB entry 4if5 coloured by chain, front view.
PDB entry 4if5 coloured by chain, side view.
PDB entry 4if5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional characterization of the α-tubulin acetyltransferase MEC-17.
Davenport AM, Collins LN, Chiu H, Minor PJ, Sternberg PW, Hoelz A
J Mol Biol 426 2605-16 (2014)
PMID: 24846647

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-178273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tubulin N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 196 amino acids
Theoretical weight: 22.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SQI0 (Residues: 1-193; Coverage: 46%)
Gene names: ATAT1, C6orf134, MEC17, Nbla00487
Sequence domains: GNAT acetyltransferase, Mec-17
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:
Ligand CL 1 x CL
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21212
Unit cell:
a: 41.747Å b: 122.297Å c: 37.541Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.178 0.214
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Tubulin acetylation: responsible enzymes, biological functions and human diseases.
Li et al. (2015)
7 more

1 mention without citation

Structural and functional characterization of the α-tubulin acetyltransferase MEC-17.
Davenport et al. (2014)