› 4f0y

X-ray diffraction
2.56Å resolution

Crystal structure of aminoglycoside antibiotic 6'-N-acetyltransferase AAC(6')-IG from Acinetobacter haemolyticus, apo

Released:
DOI: 10.2210/pdb4f0y/pdb
PDB entry 4f0y coloured by chain, front view.
PDB entry 4f0y coloured by chain, side view.
PDB entry 4f0y coloured by chain, top view.
Source organism: Acinetobacter haemolyticus
Primary publication:
Structural and Biochemical Characterization of Acinetobacter spp. Aminoglycoside Acetyltransferases Highlights Functional and Evolutionary Variation among Antibiotic Resistance Enzymes.
Stogios PJ, Kuhn ML, Evdokimova E, Law M, Courvalin P, Savchenko A
ACS Infect Dis 3 132-143 (2017)
PMID: 27785912

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + kanamycin-B = CoA + N(6')-acetylkanamycin-B
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoglycoside N(6')-acetyltransferase type 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 166 amino acids
Theoretical weight: 18.9 KDa
Source organism: Acinetobacter haemolyticus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q44057 (Residues: 1-145; Coverage: 100%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand CL 3 x CL
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 37.963Å b: 44.018Å c: 46.576Å
α: 83.19° β: 87.44° γ: 72.65°
R-values:
R R work R free
0.184 0.181 0.24
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Antibiotic Resistance Mechanisms in Bacteria: Relationships Between Resistance Determinants of Antibiotic Producers, Environmental Bacteria, and Clinical Pathogens.
Peterson et al. (2018)
2 more

3 mentions without citation

Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections.
Labby et al. (2013)
2 more