› 4gs4

X-ray diffraction
2.11Å resolution

Structure of the alpha-tubulin acetyltransferase, alpha-TAT1

Released:
DOI: 10.2210/pdb4gs4/pdb
PDB entry 4gs4 coloured by chain, front view.
PDB entry 4gs4 coloured by chain, side view.
PDB entry 4gs4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the α-tubulin acetyltransferase, αTAT1, and implications for tubulin-specific acetylation.
Friedmann DR, Aguilar A, Fan J, Nachury MV, Marmorstein R
Proc Natl Acad Sci U S A 109 19655-60 (2012)
PMID: 23071314

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: 240 amino acids
Theoretical weight: 27.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SQI0 (Residues: 2-236; Coverage: 56%)
Gene names: ATAT1, C6orf134, MEC17, Nbla00487
Sequence domains: GNAT acetyltransferase, Mec-17
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
No bound ligands
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C222
Unit cell:
a: 97.931Å b: 130.668Å c: 37.423Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.227 0.253
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

7 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
6 more