14gs
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GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1
OverviewOverview
Three-dimensional structures of the apo form of human pi class glutathione, transferase have been determined by X-ray crystallography. The structures, suggest the enzyme recognizes its substrate, glutathione, by an, induced-fit mechanism. Compared to complexed forms of the enzyme, the, environment around the catalytic residue, Tyr 7, remains unchanged in the, apoenzyme. This observation supports the view that Tyr 7 does not act as a, general base in the reaction mechanism. The observed cooperativity of the, dimeric enzyme may be due to the movements of a helix that forms one wall, of the active site and, in particular, to movements of a tyrosine residue, that is located in the subunit interface.
About this StructureAbout this Structure
14GS is a Single protein structure of sequence from Homo sapiens with MES as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
ReferenceReference
Evidence for an induced-fit mechanism operating in pi class glutathione transferases., Oakley AJ, Lo Bello M, Ricci G, Federici G, Parker MW, Biochemistry. 1998 Jul 14;37(28):9912-7. PMID:9665696
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