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TitleCharacterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis.
Journal, issue, pagesBiochemistry, Vol. 46, Page 13407-13414, Year 2007
Publish dateJul 14, 2007 (structure data deposition date)
AuthorsMorrow, A.L. / Williams, K. / Sand, A. / Boanca, G. / Barycki, J.J.
External linksBiochemistry / PubMed:17960917
MethodsX-ray diffraction
Resolution1.55 - 1.6 Å
Structure data

PDB-2qm6:
Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase in Complex with Glutamate
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-2qmc:
Crystal Structure of Helicobacter Pylori Gamma-Glutamyltranspeptidase T380A Mutant
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

Chemicals

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-HOH:
WATER

ChemComp-GTB:
S-(P-NITROBENZYL)GLUTATHIONE

Source
  • helicobacter pylori (bacteria)
KeywordsTRANSFERASE / NTN-HYDROLASE / GLUTAMYLTRANSPEPTIDASE

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