1gsu
From Proteopedia
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'''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION''' | '''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION''' | ||
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[[Category: Sun, Y J.]] | [[Category: Sun, Y J.]] | ||
[[Category: Tam, M F.]] | [[Category: Tam, M F.]] | ||
| - | [[Category: | + | [[Category: Detoxification enzyme]] |
| - | [[Category: | + | [[Category: Glutathione s-transferase]] |
| - | [[Category: | + | [[Category: S-hexyl glutathione]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:57:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:57, 2 May 2008
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. 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 Page seeded by OCA on Fri May 2 17:57:54 2008
