14GS

GLUTATHIONE S-TRANSFERASE P1-1 APO FORM 1

Summary for 14GS

• Entry DOI: 10.2210/pdb14gs/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
• Functional Keywords: transferase, apoenzyme, detoxification
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : P09211
• Total number of polymer chains: 2
• Total formula weight: 47146.01

Authors

Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W. (deposition date: 1997-11-29, release date: 1999-01-13, Last modification date: 2024-05-22)

Primary citation

Oakley, A.J.,Lo Bello, M.,Ricci, G.,Federici, G.,Parker, M.W.
Evidence for an induced-fit mechanism operating in pi class glutathione transferases.
Biochemistry, 37:9912-9917, 1998

PubMed Abstract: 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.

PubMed: 9665696
DOI: 10.1021/bi980323w

Experimental method

X-RAY DIFFRACTION (2.8 Å)