View source for 1guk


==CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4==
<StructureSection load='1guk' size='340' side='right'caption='[[1guk]], [[Resolution|resolution]] 2.90&Aring;' 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]] 2.9&#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=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].
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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1guk" style="background-color:#fffaf0;"></div>

==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]]