1gsu

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1gsu, resolution 1.94Å

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AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION

Overview

Glutathione S-transferase cGSTM1-1, an avian class-mu enzyme with high, sequence identity with rGSTM3-3, was expressed heterologously in, Escherichia coli. The three-dimensional structure of this protein that, co-crystallized with an inhibitor, S-hexylglutathione, was determined by, the molecular replacement method and refined to 1.94 A resolution. The, three-dimensional structure and the folding topology of the dimeric, cGSTM1-1 closely resembles those of other class-mu GSTs. The bound, inhibitor, S-hexylglutathione, orients in disparate directions in the two, subunits. The combined space occupied by the hexyl moiety of the, inhibitors overlaps with that reported for rGSTM1-1 co-crystallized with, (9 S,10 S)-9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene., Conformational differences at a flexible loop (residue 35 to 40) were also, observed between the crystal structures of cGSTM1-1 and rGSTM1-1.cGSTM1-1, has the highest epoxidase activity among all the class-mu enzymes, reported. Tyr115, has been identified as a residue that participates in, the epoxidase activity of class-mu glutathione S-transferase and is, conserved in cGSTM1-1. The epoxidase and trans-4-phenyl-3-buten-2-one, conjugating activity of cGSTM1-1 are decreased drastically but not, abolished by replacing Tyr115 with phenylalanine. The specificity constant, of the cGSTM1-1(Y115F) mutant, with 1-chloro-2,4-dinitrobenzene as, substrate, is 15-fold higher than that of the wild-type enzyme.

About this Structure

1GSU is a Single protein structure of sequence from Gallus gallus with GTX as ligand. Active as Glutathione transferase, with EC number 2.5.1.18 Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of an avian class-mu glutathione S-transferase, cGSTM1-1 at 1.94 A resolution., Sun YJ, Kuan IC, Tam MF, Hsiao CD, J Mol Biol. 1998 Apr 24;278(1):239-52. PMID:9571047

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