› 2fm7

X-ray diffraction
2.8Å resolution

Evolution of Enzymatic Activity in the Tautomerase Superfamily: Mechanistic and Structural Consequences of the L8R Mutation in 4-Oxalocrotonate Tautomerase

Released:
DOI: 10.2210/pdb2fm7/pdb
PDB entry 2fm7 coloured by chain, front view.
PDB entry 2fm7 coloured by chain, side view.
PDB entry 2fm7 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase.
Poelarends GJ, Almrud JJ, Serrano H, Darty JE, Johnson WH, Hackert ML, Whitman CP
Biochemistry 45 7700-8 (2006)
PMID: 16784221

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 analysis Details

Assemblies composition:
homo hexamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169563 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-hydroxymuconate tautomerase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 62 amino acids
Theoretical weight: 6.77 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01468 (Residues: 2-62; Coverage: 97%)
Gene name: xylH
Sequence domains: Tautomerase enzyme
Structure domains: Macrophage Migration Inhibitory Factor

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P63
Unit cell:
a: 80.863Å b: 80.863Å c: 117.038Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.23 0.301
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Computational enzyme design.
Kiss et al. (2013)
5 more

1 mention without citation

Evolution of enzymatic activity in the tautomerase superfamily: mechanistic and structural consequences of the L8R mutation in 4-oxalocrotonate tautomerase.
Poelarends et al. (2006)