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[[Image:1eog.gif|left|200px]]<br /><applet load="1eog" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1eog, resolution 2.1&Aring;" />
'''CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE==
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.
<StructureSection load='1eog' size='340' side='right'caption='[[1eog]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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>
== 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/eo/1eog_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=1eog ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOG OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Reference==
<references/>
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]
__TOC__
[[Category: Glutathione transferase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Aceto, A.]]
[[Category: Aceto A]]
[[Category: Cocco, R.]]
[[Category: Cocco R]]
[[Category: Dragani, B.]]
[[Category: Dragani B]]
[[Category: Mannervik, B.]]
[[Category: Mannervik B]]
[[Category: McKinstry, W J.]]
[[Category: McKinstry WJ]]
[[Category: Oakley, A J.]]
[[Category: Oakley AJ]]
[[Category: Parker, M W.]]
[[Category: Parker MW]]
[[Category: Rossjohn, J.]]
[[Category: Rossjohn J]]
[[Category: Stenberg, G.]]
[[Category: Stenberg G]]
[[Category: glutathione transferase]]
[[Category: helix capping mutant (s149a)]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:53 2008''

Latest revision as of 07:05, 7 February 2024

CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE

1eog, resolution 2.10Å

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