› 1cb7

X-ray diffraction
2Å resolution

GLUTAMATE MUTASE FROM CLOSTRIDIUM COCHLEARIUM RECONSTITUTED WITH METHYL-COBALAMIN

Released:
DOI: 10.2210/pdb1cb7/pdb
PDB entry 1cb7 coloured by chain, front view.
PDB entry 1cb7 coloured by chain, side view.
PDB entry 1cb7 coloured by chain, top view.
Source organism: Clostridium cochlearium
Primary publication:
Glutamate mutase from Clostridium cochlearium: the structure of a coenzyme B12-dependent enzyme provides new mechanistic insights.
Reitzer R, Gruber K, Jogl G, Wagner UG, Bothe H, Buckel W, Kratky C
Structure 7 891-902 (1999)
PMID: 10467146

Function and Biology Details

Reaction catalysed: 
L-threo-3-methylaspartate = L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160345 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutamate mutase sigma subunit Chains: A, C
Molecule details ›
Chains: A, C
Length: 137 amino acids
Theoretical weight: 14.83 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
  • Canonical: P80078 (Residues: 1-137; Coverage: 100%)
Gene name: glmS
Sequence domains: B12 binding domain
Structure domains: Cobalamin-binding domain
Glutamate mutase epsilon subunit Chains: B, D
Molecule details ›
Chains: B, D
Length: 483 amino acids
Theoretical weight: 53.62 KDa
Source organism: Clostridium cochlearium
Expression system: Escherichia coli
UniProt:
  • Canonical: P80077 (Residues: 1-483; Coverage: 100%)
Gene name: glmE
Sequence domains: Methylaspartate mutase E chain (MutE)
Structure domains:

Ligands and Environments


Cofactor: Ligand COB 2 x COB
1 bound ligand:
Ligand TAR 2 x TAR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P21
Unit cell:
a: 64.33Å b: 113.14Å c: 108.61Å
α: 90° β: 95.62° γ: 90°
R-values:
R R work R free
0.16 not available 0.218
Expression system: Escherichia coli

Quick links

Citations

19 review citations

The many faces of vitamin B12: catalysis by cobalamin-dependent enzymes.
Banerjee et al. (2003)
18 more

6 mentions without citation

Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily.
Chatterjee et al. (2008)
5 more