› 1xey

X-ray diffraction
2.05Å resolution

Crystal structure of the complex of Escherichia coli GADA with glutarate at 2.05 A resolution

Released:
DOI: 10.2210/pdb1xey/pdb
PDB entry 1xey coloured by chain, front view.
PDB entry 1xey coloured by chain, side view.
PDB entry 1xey coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of Escherichia coli glutamate decarboxylase (GADalpha) in complex with glutarate at 2.05 angstroms resolution.
Dutyshev DI, Darii EL, Fomenkova NP, Pechik IV, Polyakov KM, Nikonov SV, Andreeva NS, Sukhareva BS
Acta Crystallogr D Biol Crystallogr 61 230-5 (2005)
PMID: 15735332

Function and Biology Details

Reaction catalysed: 
L-glutamate = 4-aminobutanoate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159686 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate decarboxylase alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 466 amino acids
Theoretical weight: 52.74 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P69908 (Residues: 1-466; Coverage: 100%)
Gene names: JW3485, b3517, gadA, gadS
Sequence domains: Pyridoxal-dependent decarboxylase conserved domain
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
Ligand ACT 2 x ACT
Ligand GUA 2 x GUA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-6
Spacegroup: R3
Unit cell:
a: 117.1Å b: 117.1Å c: 196.4Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.151 0.148 0.199
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

Mechanisms of acid resistance in Escherichia coli.
Kanjee et al. (2013)
2 more

3 mentions without citation

The E. coli sirtuin CobB shows no preference for enzymatic and nonenzymatic lysine acetylation substrate sites.
AbouElfetouh et al. (2015)
2 more