1gsu: Difference between revisions

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New page: left|200px<br /><applet load="1gsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsu, resolution 1.94Å" /> '''AN AVIAN CLASS-MU GL...
 
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[[Image:1gsu.gif|left|200px]]<br /><applet load="1gsu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1gsu.gif|left|200px]]<br /><applet load="1gsu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1gsu, resolution 1.94&Aring;" />
caption="1gsu, resolution 1.94&Aring;" />
'''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION'''<br />
'''AN AVIAN CLASS-MU GLUTATHIONE S-TRANSFERASE, CGSTM1-1 AT 1.94 ANGSTROM RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1GSU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with GTX as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSU OCA].  
1GSU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=GTX:'>GTX</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSU OCA].  


==Reference==
==Reference==
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[[Category: Glutathione transferase]]
[[Category: Glutathione transferase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Hsiao, C.D.]]
[[Category: Hsiao, C D.]]
[[Category: Kuan, C.]]
[[Category: Kuan, C.]]
[[Category: Sun, Y.J.]]
[[Category: Sun, Y J.]]
[[Category: Tam, M.F.]]
[[Category: Tam, M F.]]
[[Category: GTX]]
[[Category: GTX]]
[[Category: detoxification enzyme]]
[[Category: detoxification enzyme]]
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[[Category: s-hexyl glutathione]]
[[Category: s-hexyl glutathione]]


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