› 1r6w

X-ray diffraction
1.62Å resolution

Crystal structure of the K133R mutant of o-Succinylbenzoate synthase (OSBS) from Escherichia coli. Complex with SHCHC

Released:
DOI: 10.2210/pdb1r6w/pdb
PDB entry 1r6w coloured by chain, front view.
PDB entry 1r6w coloured by chain, side view.
PDB entry 1r6w coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli.
Klenchin VA, Taylor Ringia EA, Gerlt JA, Rayment I
Biochemistry 42 14427-33 (2003)
PMID: 14661953

Function and Biology Details

Reaction catalysed: 
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151369 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
o-succinylbenzoate synthase Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 35.77 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P29208 (Residues: 1-320; Coverage: 100%)
Gene names: JW2256, b2261, menC
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand 164 1 x 164
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P21212
Unit cell:
a: 72.2Å b: 82.9Å c: 56.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.2
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity.
Gerlt et al. (2005)
5 other articles

1 mention without citation

Divergent evolution of ligand binding in the o-succinylbenzoate synthase family.
Odokonyero et al. (2013)