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TitleDirected Evolution of Tau Class Glutathione Transferases Reveals a Site that Regulates Catalytic Efficiency and Masks Cooperativity.
Journal, issue, pagesBiochem. J., Vol. 473, Page 559-, Year 2016
Publish dateFeb 4, 2015 (structure data deposition date)
AuthorsAxarli, I. / Muleta, A.W. / Vlachakis, D. / Kossida, S. / Kotzia, G. / Maltezos, A. / Dhavala, P. / Papageorgiou, A.C. / Labrou, N.E.
External linksBiochem. J. / PubMed:26637269
MethodsX-ray diffraction
Resolution1.75 Å
Structure data

PDB-5agy:
CRYSTAL STRUCTURE OF A TAU CLASS GST MUTANT FROM GLYCINE
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-4NM:
4-NITROPHENYL METHANETHIOL

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

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • glycine max (soybean)
KeywordsTRANSFERASE / BINDING SITE / CATALYTIC DOMAIN / ENZYME / INDUCTION / DETOXIFICATION / HERBICIDES / KINETICS / SITE-DIRECTED MUTAGENESIS / SOY BEANS / GLUTATHIONE TRANSFERASE / PROTEIN STABILITY / CATALYTIC MECHANISM / XENOBIOTIC BINDING / ALLOSTERISM

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