› 3a2y

X-ray diffraction
1.95Å resolution

E. coli Gsp amidase C59A complexed with Gsp

Released:
DOI: 10.2210/pdb3a2y/pdb
PDB entry 3a2y coloured by chain, front view.
PDB entry 3a2y coloured by chain, side view.
PDB entry 3a2y coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases.
Pai CH, Wu HJ, Lin CH, Wang AH
Protein Sci 20 557-66 (2011)
PMID: 21226054

Function and Biology Details

Reactions catalysed: 
Glutathionylspermidine + H(2)O = glutathione + spermidine
Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-142485 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutathionylspermidine synthetase/amidase Chain: A
Molecule details ›
Chain: A
Length: 197 amino acids
Theoretical weight: 22.26 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AES0 (Residues: 1-197; Coverage: 32%)
Gene names: JW2956, b2988, gsp, gss
Sequence domains: CHAP domain
Structure domains: endopeptidase domain like (from Nostoc punctiforme)

Ligands and Environments


Cofactor: Ligand TS5 1 x TS5
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P6422
Unit cell:
a: 83.962Å b: 83.962Å c: 104.937Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Glutathionylspermidine in the modification of protein SH groups: the enzymology and its application to study protein glutathionylation.
Lin et al. (2015)
3 other articles

3 mentions without citation

Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent amidohydrolases/peptidases.
Pai et al. (2011)
2 more