› 3quo

X-ray diffraction
1.58Å resolution

Crystal structure of fosfomycin resistance kinase FomA from Streptomyces wedmorensis complexed with ATP and fosfomycin

Released:
DOI: 10.2210/pdb3quo/pdb
PDB entry 3quo coloured by chain, front view.
PDB entry 3quo coloured by chain, side view.
PDB entry 3quo coloured by chain, top view.
Source organism: Streptomyces wedmorensis
Primary publication:
Structural and biochemical insights into the mechanism of fosfomycin phosphorylation by fosfomycin resistance kinase FomA.
Pakhomova S, Bartlett SG, Doerner PA, Newcomer ME
Biochemistry 50 6909-19 (2011)
PMID: 21728358

Function and Biology Details

Reaction catalysed: 
ATP + 3-methylbut-3-en-1-yl phosphate = ADP + 3-methylbut-3-en-1-yl diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176325 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isopentenyl phosphate kinase Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 30.88 KDa
Source organism: Streptomyces wedmorensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q56187 (Residues: 1-266; Coverage: 100%)
Gene name: fomA
Sequence domains: Amino acid kinase family
Structure domains: Acetylglutamate kinase-like

Ligands and Environments

2 bound ligands:
Ligand ATP 1 x ATP
Ligand FCN 1 x FCN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CAMD BEAMLINE GCPCC
Spacegroup: P3221
Unit cell:
a: 87.33Å b: 87.33Å c: 78.54Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.162 0.161 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Fosfomycin induced structural change in fosfomycin resistance kinases FomA: molecular dynamics and molecular docking studies.
Wu et al. (2014)
1 more

2 mentions without citation

The Streptomyces-produced antibiotic fosfomycin is a promiscuous substrate for archaeal isopentenyl phosphate kinase.
Mabanglo et al. (2012)
1 more