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TitleStructures of two bifunctional gamma-Glutamate-cysteine Ligase/Glutathione synthetases (GshF) reveal a novel hybrid ATP-grasp fold
Journal, issue, pagesTo be Published
Publish dateFeb 2, 2010 (structure data deposition date)
AuthorsStout, J. / De Vos, D. / Vergauwen, B. / Savvides, S.N.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution2.95 - 3.2 Å
Structure data

PDB-3ln6:
Crystal structure of a bifunctional glutathione synthetase from Streptococcus agalactiae
Method: X-RAY DIFFRACTION / Resolution: 2.95 Å

PDB-3ln7:
Crystal structure of a bifunctional glutathione synthetase from Pasteurella multocida
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • streptococcus agalactiae serogroup v (bacteria)
  • pasteurella multocida (bacteria)
KeywordsLIGASE / gamma-glutamyl cysteine ligase domain / ATP-grasp domain / hybrid enzyme / ATP-binding / Glutathione biosynthesis / Magnesium / Manganese / Metal-binding / Multifunctional enzyme / Nucleotide-binding / gamma-glutamylcysteine ligase domain

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