1eoh: Difference between revisions

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[[Image:1eoh.gif|left|200px]]


<!--
==GLUTATHIONE TRANSFERASE P1-1==
The line below this paragraph, containing "STRUCTURE_1eoh", creates the "Structure Box" on the page.
<StructureSection load='1eoh' size='340' side='right'caption='[[1eoh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1eoh]] is a 8 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=1EOH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EOH FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1eoh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eoh OCA], [https://pdbe.org/1eoh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eoh RCSB], [https://www.ebi.ac.uk/pdbsum/1eoh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eoh ProSAT]</span></td></tr>
{{STRUCTURE_1eoh|  PDB=1eoh |  SCENE= }}
</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/1eoh_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=1eoh ConSurf].
<div style="clear:both"></div>


'''GLUTATHIONE TRANSFERASE P1-1'''
==See Also==
 
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1EOH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EOH OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/10970734 10970734]
[[Category: Glutathione transferase]]
[[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]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:20:52 2008''

Latest revision as of 07:05, 7 February 2024

GLUTATHIONE TRANSFERASE P1-1

1eoh, resolution 2.50Å

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