1gsf
From Proteopedia
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GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID
Overview
BACKGROUND: Glutathione transferases (GSTs) constitute a family of, isoenzymes that catalyze the conjugation of the tripeptide glutathione, with a wide variety of hydrophobic compounds bearing an electrophilic, functional group. Recently, a number of X-ray structures have been, reported which have defined both the glutathione- and the, substrate-binding sites in these enzymes. The structure of the, glutathione-free enzyme from a mammalian source has not, however, been, reported previously. RESULTS: We have solved structures of a human, alpha-class GST, isoenzyme A1-1, both in the unliganded form and in, complexes with the inhibitor ethacrynic acid and its glutathione, conjugate. These structures have been refined to resolutions of 2.5 A, 2.7, A and 2.0 A respectively. Both forms of the inhibitor are clearly present, in the associated electron density. CONCLUSIONS: The major differences, among the three structures reported here involve the C-terminal, alpha-helix, which is a characteristic of the alpha-class enzyme. This, helix forms a lid over the active site when the hydrophobic substrate, binding site (H-site) is occupied but it is otherwise disordered., Ethacrynic acid appears to bind in a non-productive mode in the absence of, the coenzyme glutathione.
About this Structure
1GSF is a Single protein structure of sequence from Homo sapiens with EAA as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.
Reference
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:8591048
Page seeded by OCA on Mon Nov 12 17:08:44 2007
