1GSY

GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE

Summary for 1GSY

• Entry DOI: 10.2210/pdb1gsy/pdb
• Descriptor: GLUTATHIONE S-TRANSFERASE CLASS PI, GLUTATHIONE (3 entities in total)
• Functional Keywords: transferase, multigene family
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 47622.58

Authors

Parraga, A.,Garcia-Saez, I.,Coll, M. (deposition date: 1996-10-25, release date: 1997-11-19, Last modification date: 2024-05-22)

Primary citation

Parraga, A.,Garcia-Saez, I.,Walsh, S.B.,Mantle, T.J.,Coll, M.
The three-dimensional structure of a class-Pi glutathione S-transferase complexed with glutathione: the active-site hydration provides insights into the reaction mechanism.
Biochem.J., 333 ( Pt 3):811-816, 1998

PubMed Abstract: The structure of mouse liver glutathione S-transferase P1-1 complexed with its substrate glutathione (GSH) has been determined by X-ray diffraction analysis. No conformational changes in the glutathione moiety or in the protein, other than small adjustments of some side chains, are observed when compared with glutathione adduct complexes. Our structure confirms that the role of Tyr-7 is to stabilize the thiolate by hydrogen bonding and to position it in the right orientation. A comparison of the enzyme-GSH structure reported here with previously described structures reveals rearrangements in a well-defined network of water molecules in the active site. One of these water molecules (W0), identified in the unliganded enzyme (carboxymethylated at Cys-47), is displaced by the binding of GSH, and a further water molecule (W4) is displaced following the binding of the electrophilic substrate and the formation of the glutathione conjugate. The possibility that one of these water molecules participates in the proton abstraction from the glutathione thiol is discussed.

PubMed: 9677344

Experimental method

X-RAY DIFFRACTION (2.44 Å)