1guk
From Proteopedia
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| - | [[Image:1guk.gif|left|200px]]<br /><applet load="1guk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1guk, resolution 2.9Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4== |
| + | <StructureSection load='1guk' size='340' side='right'caption='[[1guk]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1guk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GUK 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]] 2.9Å</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=1guk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1guk OCA], [https://pdbe.org/1guk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1guk RCSB], [https://www.ebi.ac.uk/pdbsum/1guk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1guk ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GSTA4_MOUSE GSTA4_MOUSE] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. | ||
| + | == 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/gu/1guk_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=1guk ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 A resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site. | Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification. The enzymes protect the cells against toxicants by conjugating them to glutathione. Recently, a novel subgroup of alpha-class GSTs has been identified with altered substrate specificity which is particularly important for cellular defense against oxidative stress. Here, we report the crystal structure of murine GSTA4-4, which is the first structure of a prototypical member of this subgroup. The structure was solved by molecular replacement and refined to 2.9 A resolution. It resembles the structure of other members of the GST superfamily, but reveals a distinct substrate binding site. | ||
| - | + | Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress.,Krengel U, Schroter KH, Hoier H, Arkema A, Kalk KH, Zimniak P, Dijkstra BW FEBS Lett. 1998 Feb 6;422(3):285-90. PMID:9498801<ref>PMID:9498801</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1guk" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Dijkstra BW]] | ||
| + | [[Category: Hoier H]] | ||
| + | [[Category: Krengel U]] | ||
| + | [[Category: Schroter KH]] | ||
Current revision
CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4
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