1gyr

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{{STRUCTURE_1gyr| PDB=1gyr | SCENE= }}
 
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===MUTANT FORM OF ENOYL THIOESTER REDUCTASE FROM CANDIDA TROPICALIS===
 
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{{ABSTRACT_PUBMED_12614607}}
 
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==About this Structure==
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==Mutant form of enoyl thioester reductase from Candida tropicalis==
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[[1gyr]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYR OCA].
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<StructureSection load='1gyr' size='340' side='right'caption='[[1gyr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gyr]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYR 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]] 2.6&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gyr OCA], [https://pdbe.org/1gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gyr RCSB], [https://www.ebi.ac.uk/pdbsum/1gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gyr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ETR1_CANTR ETR1_CANTR] Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.<ref>PMID:11509667</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/gy/1gyr_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=1gyr 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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Candida tropicalis enoyl thioester reductase Etr1p and the Saccharomyces cerevisiae homologue Mrf1p catalyse the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (FAS). Unlike prokaryotic enoyl thioester reductases (ETRs), which belong to the short-chain dehydrogenases/reductases (SDR), Etr1p and Mrf1p represent structurally distinguishable ETRs that belong to the medium-chain dehydrogenases/reductases (MDR) superfamily, indicating independent origin of two separate classes of ETRs. The crystal structures of Etr1p, the Etr1p-NADPH complex and the Etr1Y79Np mutant were refined to 1.70A, 2.25A and 2.60A resolution, respectively. The native fold of Etr1p was maintained in Etr1Y79Np, but the mutant had only 0.1% of Etr1p catalytic activity remaining and failed to rescue the respiratory deficient phenotype of the mrf1Delta strain. Mutagenesis of Tyr73 in Mrf1p, corresponding to Tyr79 in Etr1p, produced similar results. Our data indicate that the mitochondrial reductase activity is indispensable for respiratory function in yeast, emphasizing the significance of Mrf1p (Etr1p) and mitochondrial FAS for the integrity of the respiratory competent organelle.
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==Reference==
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Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.,Airenne TT, Torkko JM, Van den plas S, Sormunen RT, Kastaniotis AJ, Wierenga RK, Hiltunen JK J Mol Biol. 2003 Mar 14;327(1):47-59. PMID:12614607<ref>PMID:12614607</ref>
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<ref group="xtra">PMID:012614607</ref><references group="xtra"/><references/>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gyr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Candida tropicalis]]
[[Category: Candida tropicalis]]
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[[Category: Airenne, T T.]]
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[[Category: Large Structures]]
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[[Category: Hiltunen, J K.]]
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[[Category: Airenne TT]]
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[[Category: Kastaniotis, A J.]]
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[[Category: Hiltunen JK]]
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[[Category: Plas, S Van Der.]]
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[[Category: Kastaniotis AJ]]
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[[Category: Sormunen, R T.]]
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[[Category: Sormunen RT]]
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[[Category: Torkko, J M.]]
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[[Category: Torkko JM]]
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[[Category: Wierenga, R K.]]
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[[Category: Van Der Plas S]]
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[[Category: Oxidoreductase]]
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[[Category: Wierenga RK]]

Current revision

Mutant form of enoyl thioester reductase from Candida tropicalis

PDB ID 1gyr

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