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1tdi

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[[Image:1tdi.gif|left|200px]]
[[Image:1tdi.gif|left|200px]]
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{{Structure
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|PDB= 1tdi |SIZE=350|CAPTION= <scene name='initialview01'>1tdi</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1tdi", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= GSTA3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1tdi| PDB=1tdi | SCENE= }}
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|RELATEDENTRY=[[1guh|1guh]], [[1gse|1gse]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tdi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdi OCA], [http://www.ebi.ac.uk/pdbsum/1tdi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tdi RCSB]</span>
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'''Crystal Structure of hGSTA3-3 in Complex with Glutathione'''
'''Crystal Structure of hGSTA3-3 in Complex with Glutathione'''
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[[Category: Singh, S V.]]
[[Category: Singh, S V.]]
[[Category: Zimniak, P.]]
[[Category: Zimniak, P.]]
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[[Category: gst]]
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[[Category: Gst]]
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[[Category: hgsta3-3]]
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[[Category: Hgsta3-3]]
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[[Category: steroid isomerase]]
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[[Category: Steroid isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:49:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:35 2008''
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Revision as of 06:49, 3 May 2008

Image:1tdi.gif

Template:STRUCTURE 1tdi

Crystal Structure of hGSTA3-3 in Complex with Glutathione


Overview

The crystal structure of human class alpha glutathione (GSH) S-transferase A3-3 (hGSTA3-3) in complex with GSH was determined at 2.4 A. Despite considerable amino acid sequence identity with other human class alpha GSTs (e.g., hGSTA1-1), hGSTA3-3 is unique due to its exceptionally high steroid double bond isomerase activity for the transformation of Delta(5)-androstene-3,17-dione (Delta(5)-AD) to Delta(4)-androstene-3,17-dione. A comparative analysis of the active centers of hGSTA1-1 and hGSTA3-3 reveals that residues in positions 12 and 208 may contribute to their disparate isomerase activity toward Delta(5)-AD. Substitution of these two residues of hGSTA3-3 with the corresponding residues in hGSTA1-1 followed by kinetic characterization of the wild-type and the mutant enzymes supported this prediction. On the basis of our model of the hGSTA3-3.GSH.Delta(5)-AD ternary complex and available biochemical data, we propose that the thiolate group of deprotonated GSH (GS(-)) serves as a base to initiate the reaction by accepting a proton from the steroid and the nonionized hydroxyl group of catalytic residue Y9 (HO-Y9) functions as part of a proton-conducting wire to transfer a proton back to the steroid. Residue R15 may function to stabilize the deprotonated thiolate group of GSH (GS(-)), and a GSH-bound water molecule may donate a hydrogen bond to the 3-keto group of Delta(5)-AD and thus help the thiolate of GS(-) to initiate the proton transfer and the subsequent stabilization of the reaction intermediate.

About this Structure

1TDI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human glutathione S-transferase A3-3 and mechanistic implications for its high steroid isomerase activity., Gu Y, Guo J, Pal A, Pan SS, Zimniak P, Singh SV, Ji X, Biochemistry. 2004 Dec 21;43(50):15673-9. PMID:15595823 Page seeded by OCA on Sat May 3 09:49:23 2008

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