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Structure paper

TitleProtein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 25345-25353, Year 2010
Publish dateJun 5, 2009 (structure data deposition date)
AuthorsChiang, B.-Y. / Chen, T.-C. / Pai, C.-H. / Chou, C.-C. / Chen, H.-H. / Ko, T.-P. / Hsu, W.-H. / Chang, C.-Y. / Wu, W.-F. / Wang, A.H.-J. / Lin, C.-H.
External linksJ. Biol. Chem. / PubMed:20530482
MethodsX-ray diffraction
Resolution1.5 - 2.2 Å
Structure data

PDB-3a2z:
E. coli Gsp amidase Cys59 sulfenic acid
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-3a30:
E. coli Gsp amidase C59 acetate modification
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-ACT:
ACETATE ION

Source
  • escherichia coli (E. coli)
KeywordsHydrolase / Ligase / Gsp amidase / ATP-binding / Multifunctional enzyme / Nucleotide-binding

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