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1gsd

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GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM

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Retrieved from "http://52.214.119.220/wiki/index.php/1gsd"

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-[[Image:1gsd.gif|left|200px]]<br />
-<applet load="1gsd" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1gsd, resolution 2.5&Aring;" />
-'''GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM'''<br />
-==Overview==
+==GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM==
-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.
+<StructureSection load='1gsd' size='340' side='right'caption='[[1gsd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1gsd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSD FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsd OCA], [https://pdbe.org/1gsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsd RCSB], [https://www.ebi.ac.uk/pdbsum/1gsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/1gsd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gsd ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-GSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1GSD OCA].
+*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
+== References ==
-==Reference==
+<references/>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591048 8591048]
+__TOC__
-[[Category: Glutathione transferase]]
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cameron, A.D.]]
+[[Category: Cameron AD]]
-[[Category: Hermite, G.L.]]
+[[Category: Jones TA]]
-[[Category: Jones, T.A.]]
+[[Category: L'Hermite G]]
-[[Category: Sinning, I.]]
+[[Category: Sinning I]]
-[[Category: transferase (glutathione)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:08:38 2007''

1gsd

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GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM

Structural highlights

Function

Evolutionary Conservation

See Also

References

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