› 3whq

X-ray diffraction
1.85Å resolution

Crystal structure of gamma-glutamyltranspeptidase from Bacillus subtilis (crystal soaked for 0 min. in acivicin soln. )

Released:
DOI: 10.2210/pdb3whq/pdb
PDB entry 3whq coloured by chain, front view.
PDB entry 3whq coloured by chain, side view.
PDB entry 3whq coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Structure of Bacillus subtilis γ-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site-directed glutamate analogue.
Ida T, Suzuki H, Fukuyama K, Hiratake J, Wada K
OpenAccess logo Acta Crystallogr D Biol Crystallogr 70 607-14 (2014)
PMID: 24531494

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 analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157021 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase large chain Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 46.29 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P54422 (Residues: 1-402; Coverage: 67%)
Gene names: BSU18410, ggt
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase small chain Chain: B
Molecule details ›
Chain: B
Length: 185 amino acids
Theoretical weight: 20.03 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P54422 (Residues: 403-587; Coverage: 33%)
Gene names: BSU18410, ggt
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 59.633Å b: 71.664Å c: 143.746Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.214
Expression system: Escherichia coli

Quick links

Citations

7 citation in other articles

Target discovery of acivicin in cancer cells elucidates its mechanism of growth inhibition†Electronic supplementary information (ESI) available: Synthesis, cloning, protein expression, purification and biochemical assays. See DOI: 10.1039/c4sc02339k.
Kreuzer et al. (2014)
6 more

2 mentions without citation

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