› 1bjp

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF 4-OXALOCROTONATE TAUTOMERASE INACTIVATED BY 2-OXO-3-PENTYNOATE AT 2.4 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1bjp/pdb
PDB entry 1bjp coloured by chain, front view.
PDB entry 1bjp coloured by chain, side view.
PDB entry 1bjp coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Crystal structure of 4-oxalocrotonate tautomerase inactivated by 2-oxo-3-pentynoate at 2.4 A resolution: analysis and implications for the mechanism of inactivation and catalysis.
Taylor AB, Czerwinski RM, Johnson WH, Whitman CP, Hackert ML
Biochemistry 37 14692-700 (1998)
PMID: 9778344

Function and Biology Details

Reaction catalysed: 
(2Z,4E)-2-hydroxyhexa-2,4-dienedioate = (3E)-2-oxohex-3-enedioate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169566 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-hydroxymuconate tautomerase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 62 amino acids
Theoretical weight: 6.82 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01468 (Residues: 2-63; Coverage: 98%)
Gene name: xylH
Sequence domains: Tautomerase enzyme
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

1 bound ligand:
Ligand OXP 5 x OXP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: R32
Unit cell:
a: 78.7Å b: 78.7Å c: 314.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.244
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Biodegradation of aromatic compounds by Escherichia coli.
Díaz et al. (2001)
4 more

10 mentions without citation

A homodimer interface without base pairs in an RNA mimic of red fluorescent protein.
Warner et al. (2017)
9 more