4r7u

X-ray diffraction
2.45Å resolution

Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Vibrio cholerae in complex with substrate UDP-N-acetylglucosamine and the drug fosfomycin

Released:
Entry authors: Nocek B, Maltseva N, Anderson W, Joachimiak A, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Reaction catalysed:
Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine 1-carboxyvinyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 422 amino acids
Theoretical weight: 45.01 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KP62 (Residues: 1-419; Coverage: 100%)
Gene names: VC_2514, murA
Sequence domains: EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase)
Structure domains: Enolpyruvate transferase domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R3
Unit cell:
a: 204.283Å b: 204.283Å c: 118.878Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.234
Expression system: Escherichia coli BL21(DE3)