2ab6: Difference between revisions

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New page: left|200px<br /> <applet load="2ab6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ab6, resolution 2.50Å" /> '''HUMAN GLUTATHIONE S...
 
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[[Image:2ab6.gif|left|200px]]<br />
<applet load="2ab6" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ab6, resolution 2.50&Aring;" />
'''HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE'''<br />


==Overview==
==HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE==
Human glutathione-S-transferase M2-2 (hGSTM2-2) was expressed in, Escherichia coli and purified by GSH-affinity chromatography. The, recombinant enzyme and the protein isolated from human tissue were, indistinguishable based on physicochemical, enzymatic and immunological, criteria. The catalytically active dimeric hGSTM2-2 was crystallized, without GSH or other active-site ligands in two crystal forms. Diffraction, from form A crystals extends to 2.5 A and is consistent with the space, group P21 (a = 53.9, b = 81.5, c = 55.6 A, beta = 109.26 A) with two, monomers in the asymmetric unit. Diffraction from form B crystals extends, to 3 A and is consistent with a space group P212121 (a = 57.2, b = 80.7, c, = 225.9 A) with two dimers in the asymmetric unit. This is the first, report of ligand-free mu-class GST crystals, and a comparison with, liganded complexes will provide insight into the structural consequences, of substrate binding which are thought to be important for catalysis.
<StructureSection load='2ab6' size='340' side='right'caption='[[2ab6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ab6]] 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=2AB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AB6 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSM:L-GAMMA-GLUTAMYL-S-METHYLCYSTEINYLGLYCINE'>GSM</scene></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=2ab6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab6 OCA], [https://pdbe.org/2ab6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ab6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ab6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ab6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTM2_HUMAN GSTM2_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:16549767</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/ab/2ab6_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=2ab6 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2AB6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with GSM as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2AB6 OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Reference==
<references/>
Expression, crystallization and preliminary X-ray analysis of ligand-free human glutathione S-transferase M2-2., Patskovska LN, Fedorov AA, Patskovsky YV, Almo SC, Listowsky I, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):458-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9761928 9761928]
__TOC__
[[Category: Glutathione transferase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Almo, S.C.]]
[[Category: Almo SC]]
[[Category: Listowsky, I.]]
[[Category: Listowsky I]]
[[Category: Patskovsky, Y.]]
[[Category: Patskovsky Y]]
[[Category: GSM]]
[[Category: conjugation]]
[[Category: detoxification]]
[[Category: s-methylglutathione]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:48:22 2007''

Latest revision as of 07:22, 23 August 2023

HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18) complexed with S-METHYLGLUTATHIONE

2ab6, resolution 2.50Å

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