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1guk

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(New page: 200px<br /><applet load="1guk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1guk, resolution 2.9&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1guk.gif|left|200px]]<br /><applet load="1guk" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1guk, resolution 2.9&Aring;" />
 
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'''CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4==
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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.
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<StructureSection load='1guk' size='340' side='right'caption='[[1guk]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTA4_MOUSE GSTA4_MOUSE] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1guk_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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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1GUK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. 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=1GUK OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9498801 9498801]
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</div>
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[[Category: Glutathione transferase]]
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<div class="pdbe-citations 1guk" style="background-color:#fffaf0;"></div>
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[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Hoier, H.]]
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[[Category: Krengel, U.]]
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[[Category: Schroter, K.H.]]
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[[Category: crystal structure]]
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[[Category: glutathione s-transferase]]
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[[Category: gst]]
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[[Category: oxidative stress]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:17:44 2007''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Mus musculus]]
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[[Category: Dijkstra BW]]
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[[Category: Hoier H]]
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[[Category: Krengel U]]
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[[Category: Schroter KH]]

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CRYSTAL STRUCTURE OF MURINE ALPHA-CLASS GSTA4-4

PDB ID 1guk

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