› 2nqo

X-ray diffraction
1.9Å resolution

Crystal Structure of Helicobacter pylori gamma-Glutamyltranspeptidase

Released:
DOI: 10.2210/pdb2nqo/pdb
PDB entry 2nqo coloured by chain, front view.
PDB entry 2nqo coloured by chain, side view.
PDB entry 2nqo coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Autoprocessing of Helicobacter pylori gamma-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad.
Boanca G, Sand A, Okada T, Suzuki H, Kumagai H, Fukuyama K, Barycki JJ
J Biol Chem 282 534-41 (2007)
PMID: 17107958

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

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127781 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase proenzyme Chains: A, C
Molecule details ›
Chains: A, C
Length: 376 amino acids
Theoretical weight: 40.51 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: O25743 (Residues: 27-379; Coverage: 62%)
Gene name: HP_1118
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase proenzyme Chains: B, D
Molecule details ›
Chains: B, D
Length: 188 amino acids
Theoretical weight: 20.41 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli
UniProt:
  • Canonical: O25743 (Residues: 380-567; Coverage: 33%)
Gene name: HP_1118
Sequence domains: Gamma-glutamyltranspeptidase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 54.354Å b: 105.206Å c: 91.06Å
α: 90° β: 91.99° γ: 90°
R-values:
R R work R free
0.197 0.197 0.239
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Emerging regulatory paradigms in glutathione metabolism.
Liu et al. (2014)
1 more

7 mentions without citation

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