› 2io9

X-ray diffraction
2.2Å resolution

E. coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+ ,GSH and ADP

Released:
DOI: 10.2210/pdb2io9/pdb
PDB entry 2io9 coloured by chain, front view.
PDB entry 2io9 coloured by chain, side view.
PDB entry 2io9 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Dual binding sites for translocation catalysis by Escherichia coli glutathionylspermidine synthetase.
Pai CH, Chiang BY, Ko TP, Chou CC, Chong CM, Yen FJ, Chen S, Coward JK, Wang AH, Lin CH
EMBO J 25 5970-82 (2006)
PMID: 17124497

Function and Biology Details

Reactions catalysed: 
Glutathionylspermidine + H(2)O = glutathione + spermidine
Glutathione + spermidine + ATP = glutathionylspermidine + ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutathionylspermidine synthetase/amidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 619 amino acids
Theoretical weight: 70.61 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AES0 (Residues: 1-619; Coverage: 100%)
Gene names: JW2956, b2988, gsp, gss
Sequence domains:
Structure domains: endopeptidase domain like (from Nostoc punctiforme)

Ligands and Environments


Cofactor: Ligand GSH 2 x GSH
2 bound ligands:
Ligand MG 4 x MG
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 59.912Å b: 75.48Å c: 84.006Å
α: 70.442° β: 74.165° γ: 78.064°
R-values:
R R work R free
0.17 0.17 0.232
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Insights into the redox biology of Trypanosoma cruzi: Trypanothione metabolism and oxidant detoxification.
Irigoín et al. (2008)
3 more

4 mentions without citation

Divergence and convergence in enzyme evolution.
Galperin et al. (2012)
3 more