PDBsum entry 14gs

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Transferase PDB id
Protein chain
194 a.a. *
MES ×2
Waters ×5
* Residue conservation analysis

References listed in PDB file
Key reference
Title Evidence for an induced-Fit mechanism operating in pi class glutathione transferases.
Authors A.J.Oakley, M.Lo bello, G.Ricci, G.Federici, M.W.Parker.
Ref. Biochemistry, 1998, 37, 9912-9917. [DOI no: 10.1021/bi980323w]
PubMed id 9665696
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.
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