2ab6

<StructureSection load='2ab6' size='340' side='right' caption='[[2ab6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2ab6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AB6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GSM:L-GAMMA-GLUTAMYL-S-METHYLCYSTEINYLGLYCINE'>GSM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gtu|1gtu]], [[1xw5|1xw5]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GSTM2, GST4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ab6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ab6 OCA], [http://pdbe.org/2ab6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ab6 RCSB], [http://www.ebi.ac.uk/pdbsum/2ab6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ab6 ProSAT]</span></td></tr>

[[http://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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/2ab6_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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:9761928<ref>PMID:9761928</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

<div class="pdbe-citations 2ab6" style="background-color:#fffaf0;"></div>

[[Category: Glutathione transferase]]

[[Category: Human]]

[[Category: Almo, S C]]

[[Category: Listowsky, I]]

[[Category: Patskovsky, Y]]

[[Category: Transferase]]