› 2e0w

X-ray diffraction
2.55Å resolution

T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli

Released:
DOI: 10.2210/pdb2e0w/pdb
PDB entry 2e0w coloured by chain, front view.
PDB entry 2e0w coloured by chain, side view.
PDB entry 2e0w coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of the gamma-glutamyltranspeptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism.
Okada T, Suzuki H, Wada K, Kumagai H, Fukuyama K
J Biol Chem 282 2433-9 (2007)
PMID: 17135273

Function and Biology Details

Reactions catalysed: 
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148480 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione hydrolase proenzyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 556 amino acids
Theoretical weight: 59.29 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P18956 (Residues: 25-580; Coverage: 100%)
Gene names: JW3412, b3447, ggt
Sequence domains: Gamma-glutamyltranspeptidase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P43212
Unit cell:
a: 134.6Å b: 134.6Å c: 118.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.27
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration.
Ekici et al. (2008)
5 more

6 mentions without citation

Bacterial Gamma-Glutamyl Transpeptidase, an Emerging Biocatalyst: Insights Into Structure-Function Relationship and Its Biotechnological Applications.
Saini et al. (2021)
5 more