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1eog

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(New page: 200px<br /> <applet load="1eog" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eog, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1eog.gif|left|200px]]<br />
 
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<applet load="1eog" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1eog, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE==
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An N-capping box motif (Ser/Thr-Xaa-Xaa-Asp) is strictly conserved at the, beginning of helix alpha6 in the core of virtually all glutathione, transferases (GST) and GST-related proteins. It has been demonstrated that, this local motif is important in determining the alpha-helical propensity, of the isolated alpha6-peptide and plays a crucial role in the folding and, stability of GSTs. Its removal by site-directed mutagenesis generated, temperature-sensitive folding mutants unable to refold at physiological, temperature (37 degrees C). In the present work, variants of human GSTP1-1, (S150A and D153A), in which the capping residues have been substituted by, alanine, have been generated and purified for structural analysis. Thus, for the first time, temperature-sensitive folding mutants of an enzyme, expressed at a permissive temperature, have been crystallized and their, three-dimensional structures determined by X-ray crystallography. The, crystal structures of human pi class GST temperature-sensitive mutants, provide a basis for understanding the structural origin of the dramatic, effects observed on the overall stability of the enzyme at higher, temperatures upon single substitution of a capping residue.
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<StructureSection load='1eog' size='340' side='right'caption='[[1eog]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1eog]] is a 2 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=1EOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOG 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]] 2.1&#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=1eog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eog OCA], [https://pdbe.org/1eog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eog RCSB], [https://www.ebi.ac.uk/pdbsum/1eog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eog ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTP1_HUMAN GSTP1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.<ref>PMID:21668448</ref>
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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/eo/1eog_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=1eog ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1EOG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=1EOG OCA].
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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== References ==
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==Reference==
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<references/>
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Structures of thermolabile mutants of human glutathione transferase P1-1., Rossjohn J, McKinstry WJ, Oakley AJ, Parker MW, Stenberg G, Mannervik B, Dragani B, Cocco R, Aceto A, J Mol Biol. 2000 Sep 15;302(2):295-302. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10970734 10970734]
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__TOC__
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[[Category: Glutathione transferase]]
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Aceto, A.]]
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[[Category: Aceto A]]
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[[Category: Cocco, R.]]
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[[Category: Cocco R]]
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[[Category: Dragani, B.]]
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[[Category: Dragani B]]
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[[Category: Mannervik, B.]]
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[[Category: Mannervik B]]
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[[Category: McKinstry, W.J.]]
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[[Category: McKinstry WJ]]
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[[Category: Oakley, A.J.]]
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[[Category: Oakley AJ]]
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[[Category: Parker, M.W.]]
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[[Category: Parker MW]]
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[[Category: Rossjohn, J.]]
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[[Category: Rossjohn J]]
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[[Category: Stenberg, G.]]
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[[Category: Stenberg G]]
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[[Category: glutathione transferase]]
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[[Category: helix capping mutant (s149a)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:45:10 2007''
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CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE

PDB ID 1eog

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