2caq

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[[Image:2caq.gif|left|200px]]
 
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==Structure of R21L mutant of Sh28GST in complex with GSH==
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The line below this paragraph, containing "STRUCTURE_2caq", creates the "Structure Box" on the page.
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<StructureSection load='2caq' size='340' side='right'caption='[[2caq]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2caq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CAQ 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&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=GSH:GLUTATHIONE'>GSH</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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{{STRUCTURE_2caq| PDB=2caq | SCENE= }}
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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=2caq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2caq OCA], [https://pdbe.org/2caq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2caq RCSB], [https://www.ebi.ac.uk/pdbsum/2caq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2caq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GST28_SCHBO GST28_SCHBO] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.
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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/ca/2caq_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=2caq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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During turnover, the catalytic tyrosine residue (Tyr10) of the sigma class Schistosoma haematobium wild-type glutathione-S-transferase is expected to switch alternately in and out of the reduced glutathione-binding site (G-site). The Tyrout10 conformer forms a pi-cation interaction with the guanidinium group of Arg21. As in other similar glutathione-S-transferases, the catalytic Tyr has a low pKa of 7.2. In order to investigate the catalytic role of Tyr10, and the structural and functional roles of Arg21, we carried out structural studies on two Arg21 mutants (R21L and R21Q) and a Tyr10 mutant, Y10F. Our crystallographic data for the two Arg21 mutants indicate that only the Tyrout10 conformation is populated, thereby excluding a role of Arg21 in the stabilisation of the out conformation. However, Arg21 was confirmed to be catalytically important and essential for the low pKa of Tyr10. Upon comparison with structural data generated for reduced glutathione-bound and inhibitor-bound wild-type enzymes, it was observed that the orientations of Tyr10 and Arg35 are concerted and that, upon ligand binding, minor rearrangements occur within conserved residues in the active site loop. These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain.
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'''STRUCTURE OF R21L MUTANT OF SH28GST IN COMPLEX WITH GSH'''
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Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography.,Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:16777141<ref>PMID:16777141</ref>
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==Overview==
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During turnover, the catalytic tyrosine residue (Tyr10) of the sigma class Schistosoma haematobium wild-type glutathione-S-transferase is expected to switch alternately in and out of the reduced glutathione-binding site (G-site). The Tyrout10 conformer forms a pi-cation interaction with the guanidinium group of Arg21. As in other similar glutathione-S-transferases, the catalytic Tyr has a low pKa of 7.2. In order to investigate the catalytic role of Tyr10, and the structural and functional roles of Arg21, we carried out structural studies on two Arg21 mutants (R21L and R21Q) and a Tyr10 mutant, Y10F. Our crystallographic data for the two Arg21 mutants indicate that only the Tyrout10 conformation is populated, thereby excluding a role of Arg21 in the stabilisation of the out conformation. However, Arg21 was confirmed to be catalytically important and essential for the low pKa of Tyr10. Upon comparison with structural data generated for reduced glutathione-bound and inhibitor-bound wild-type enzymes, it was observed that the orientations of Tyr10 and Arg35 are concerted and that, upon ligand binding, minor rearrangements occur within conserved residues in the active site loop. These rearrangements are coupled to quaternary rigid-body movements at the dimer interface and alterations in the localisation and structural order of the C-terminal domain.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2CAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Schistosoma_haematobium Schistosoma haematobium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CAQ OCA].
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</div>
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<div class="pdbe-citations 2caq" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography., Baiocco P, Gourlay LJ, Angelucci F, Fontaine J, Herve M, Miele AE, Trottein F, Brunori M, Bellelli A, J Mol Biol. 2006 Jul 14;360(3):678-89. Epub 2006 Jun 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16777141 16777141]
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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[[Category: Glutathione transferase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Schistosoma haematobium]]
[[Category: Schistosoma haematobium]]
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[[Category: Single protein]]
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[[Category: Angelucci F]]
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[[Category: Angelucci, F.]]
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[[Category: Baiocco P]]
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[[Category: Baiocco, P.]]
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[[Category: Bellelli A]]
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[[Category: Bellelli, A.]]
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[[Category: Brunori M]]
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[[Category: Brunori, M.]]
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[[Category: Gourlay LJ]]
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[[Category: Gourlay, L J.]]
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[[Category: Miele AE]]
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[[Category: Miele, A E.]]
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[[Category: Antigen]]
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[[Category: Detoxification]]
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[[Category: Glutathione]]
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[[Category: Prostaglandin d2 synthase]]
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[[Category: Sigma class gst]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:35:42 2008''
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Current revision

Structure of R21L mutant of Sh28GST in complex with GSH

PDB ID 2caq

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