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Structure paper

TitleCrystal structures of Escherichia coli gamma-glutamyltranspeptidase in complex with azaserine and acivicin: novel mechanistic implication for inhibition by glutamine antagonists
Journal, issue, pagesJ. Mol. Biol., Vol. 380, Page 361-372, Year 2008
Publish dateSep 5, 2007 (structure data deposition date)
AuthorsWada, K. / Hiratake, J. / Irie, M. / Okada, T. / Yamada, C. / Kumagai, H. / Suzuki, H. / Fukuyama, K.
External linksJ. Mol. Biol. / PubMed:18555071
MethodsX-ray diffraction
Resolution1.65 - 2.05 Å
Structure data

PDB-2z8i:
Crystal Structure of Escherichia coli Gamma-Glutamyltranspeptidase in Complex with Azaserine
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-2z8j:
Crystal Structure of Escherichia coli gamma-Glutamyltranspeptidase in Complex with Azaserine prepared in the dark
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

PDB-2z8k:
Crystal Structure of Escherichia coli gamma-Glutamyltranspeptidase in Complex with Acivicin
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

Chemicals

ChemComp-AZS:
O-DIAZOACETYL-L-SERINE / antineoplastic, antibiotic, antagonist*YM

ChemComp-HOH:
WATER

ChemComp-AVN:
(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID / inhibitor*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Thr391 formed a covalent bond with azaserine / Acyltransferase / Glutathione biosynthesis / Zymogen / Azaserine with a diazo group / covalent bond with Thr391 / Acivicin formed a covalent bond with Thr391

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