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1gsy

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(New page: 200px<br /> <applet load="1gsy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsy, resolution 2.44&Aring;" /> '''GLUTATHIONE S-TRANS...)
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[[Image:1gsy.gif|left|200px]]<br />
 
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<applet load="1gsy" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gsy, resolution 2.44&Aring;" />
 
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'''GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE'''<br />
 
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==Overview==
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==GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE==
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The three-dimensional crystal structure of pi class glutathione, S-transferase YfYf from mouse liver complexed with the inhibitor, S-(p-nitrobenzyl)glutathione has been determined at 1.8 A resolution by, X-ray diffraction. In addition two complexes with glutathione sulphonic, acid and S-hexylglutathione have been determined at resolutions of 1.9 and, 2.2 A, respectively. The high resolution of the, S-(p-nitrobenzyl)glutathione complex allows a detailed analysis of the, active site including the hydrophobic (H-) subsite. The nitrobenzyl moiety, occupies a hydrophobic pocket with its aromatic ring sandwiched between, Phe8 and the hydroxyl group of Tyr108. An insertion of two residues Gly41, and Leu42, with respect to the pig enzyme, splits helix alpha B into an, alpha-helix and a 3(10) ... [[http://ispc.weizmann.ac.il/pmbin/getpm?8145243 (full description)]]
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<StructureSection load='1gsy' size='340' side='right'caption='[[1gsy]], [[Resolution|resolution]] 2.44&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gsy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSY 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]] 2.44&#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=GSH:GLUTATHIONE'>GSH</scene></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=1gsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsy OCA], [https://pdbe.org/1gsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsy RCSB], [https://www.ebi.ac.uk/pdbsum/1gsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GSTP1_MOUSE GSTP1_MOUSE] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity).
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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/gs/1gsy_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=1gsy 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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The structure of mouse liver glutathione S-transferase P1-1 complexed with its substrate glutathione (GSH) has been determined by X-ray diffraction analysis. No conformational changes in the glutathione moiety or in the protein, other than small adjustments of some side chains, are observed when compared with glutathione adduct complexes. Our structure confirms that the role of Tyr-7 is to stabilize the thiolate by hydrogen bonding and to position it in the right orientation. A comparison of the enzyme-GSH structure reported here with previously described structures reveals rearrangements in a well-defined network of water molecules in the active site. One of these water molecules (W0), identified in the unliganded enzyme (carboxymethylated at Cys-47), is displaced by the binding of GSH, and a further water molecule (W4) is displaced following the binding of the electrophilic substrate and the formation of the glutathione conjugate. The possibility that one of these water molecules participates in the proton abstraction from the glutathione thiol is discussed.
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==About this Structure==
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The three-dimensional structure of a class-Pi glutathione S-transferase complexed with glutathione: the active-site hydration provides insights into the reaction mechanism.,Parraga A, Garcia-Saez I, Walsh SB, Mantle TJ, Coll M Biochem J. 1998 Aug 1;333 ( Pt 3):811-6. PMID:9677344<ref>PMID:9677344</ref>
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1GSY is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]] with GTT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1GSY OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Molecular structure at 1.8 A of mouse liver class pi glutathione S-transferase complexed with S-(p-nitrobenzyl)glutathione and other inhibitors., Garcia-Saez I, Parraga A, Phillips MF, Mantle TJ, Coll M, J Mol Biol. 1994 Apr 1;237(3):298-314. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8145243 8145243]
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</div>
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[[Category: Mus musculus]]
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<div class="pdbe-citations 1gsy" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Coll, M.]]
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[[Category: Garcia-Saez, I.]]
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[[Category: Parraga, A.]]
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[[Category: GTT]]
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[[Category: 3d-structure]]
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[[Category: multigene family]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:51:30 2007''
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==See Also==
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*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
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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]]
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[[Category: Mus musculus]]
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[[Category: Coll M]]
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[[Category: Garcia-Saez I]]
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[[Category: Parraga A]]

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GLUTATHIONE S-TRANSFERASE YFYF, CLASS PI, COMPLEXED WITH GLUTATHIONE

PDB ID 1gsy

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