› 4nv7

X-ray diffraction
2.02Å resolution

Crystal Structure of Mesorhizobium Loti Arylamine N-acetyltransferase 1 In Complex With CoA

Released:
DOI: 10.2210/pdb4nv7/pdb
PDB entry 4nv7 coloured by chain, front view.
PDB entry 4nv7 coloured by chain, side view.
PDB entry 4nv7 coloured by chain, top view.
Source organism: Mesorhizobium japonicum MAFF 303099
Primary publication:
Insight into cofactor recognition in arylamine N-acetyltransferase enzymes: structure of Mesorhizobium loti arylamine N-acetyltransferase in complex with coenzyme A.
Xu X, Li de la Sierra-Gallay I, Kubiak X, Duval R, Chaffotte AF, Dupret JM, Haouz A, Rodrigues-Lima F
Acta Crystallogr D Biol Crystallogr 71 266-73 (2015)
PMID: 25664736

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-189141 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylamine N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 312 amino acids
Theoretical weight: 34.36 KDa
Source organism: Mesorhizobium japonicum MAFF 303099
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q98D42 (Residues: 1-278; Coverage: 100%)
Gene name: mlr4870
Sequence domains: N-acetyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand COA 2 x COA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P212121
Unit cell:
a: 53.5Å b: 114.86Å c: 115.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.221
Expression system: Escherichia coli BL21

Quick links

Citations

5 citation in other articles

Identification of cancer chemopreventive isothiocyanates as direct inhibitors of the arylamine N-acetyltransferase-dependent acetylation and bioactivation of aromatic amine carcinogens.
Duval et al. (2016)
4 more

2 mentions without citation

Comparative Investigation of 15 Xenobiotic-Metabolizing N-Acetyltransferase (NAT) Homologs from Bacteria.
Garefalaki et al. (2021)
1 more