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1n9g

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[[Image:1n9g.png|left|200px]]
 
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==Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis==
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The line below this paragraph, containing "STRUCTURE_1n9g", creates the "Structure Box" on the page.
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<StructureSection load='1n9g' size='340' side='right'caption='[[1n9g]], [[Resolution|resolution]] 1.98&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'>[[1n9g]] is a 6 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=1N9G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9G 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]] 1.98&#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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1n9g| PDB=1n9g | 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=1n9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9g OCA], [https://pdbe.org/1n9g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9g RCSB], [https://www.ebi.ac.uk/pdbsum/1n9g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9g ProSAT]</span></td></tr>
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</table>
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'''Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis'''
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== Function ==
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[https://www.uniprot.org/uniprot/ETR2_CANTR ETR2_CANTR] Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.
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== Evolutionary Conservation ==
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==Overview==
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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/n9/1n9g_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=1n9g 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 ==
Here we report on the cloning of a Candida tropicalis gene, ETR2, that is closely related to ETR1. Both genes encode enzymatically active 2-enoyl thioester reductases involved in mitochondrial synthesis of fatty acids (fatty acid synthesis type II) and respiratory competence. The 5'- and 3'-flanking (coding) regions of ETR2 and ETR1 are about 90% (97%) identical, indicating that the genes have evolved via gene duplication. The gene products differ in three amino acid residues: Ile67 (Val), Ala92 (Thr), and Lys251 (Arg) in Etr2p (Etr1p). Quantitative PCR analysis and reverse transcriptase-PCR indicated that both genes were expressed about equally in fermenting and ETR1 predominantly respiring yeast cells. Like the situation with ETR1, expression of ETR2 in respiration-deficient Saccharomyces cerevisiae mutant cells devoid of Ybr026p/Etr1p was able to restore growth on glycerol. Triclosan that is used as an antibacterial agent against fatty acid synthesis type II 2-enoyl thioester reductases inhibited growth of FabI overexpressing mutant yeast cells but was not able to inhibit respiratory growth of the ETR2- or ETR1-complemented mutant yeast cells. Resolving of crystal structures obtained via Etr2p and Etr1p co-crystallization indicated that all possible dimer variants occur in the same asymmetric unit, suggesting that similar dimer formation also takes place in vivo.
Here we report on the cloning of a Candida tropicalis gene, ETR2, that is closely related to ETR1. Both genes encode enzymatically active 2-enoyl thioester reductases involved in mitochondrial synthesis of fatty acids (fatty acid synthesis type II) and respiratory competence. The 5'- and 3'-flanking (coding) regions of ETR2 and ETR1 are about 90% (97%) identical, indicating that the genes have evolved via gene duplication. The gene products differ in three amino acid residues: Ile67 (Val), Ala92 (Thr), and Lys251 (Arg) in Etr2p (Etr1p). Quantitative PCR analysis and reverse transcriptase-PCR indicated that both genes were expressed about equally in fermenting and ETR1 predominantly respiring yeast cells. Like the situation with ETR1, expression of ETR2 in respiration-deficient Saccharomyces cerevisiae mutant cells devoid of Ybr026p/Etr1p was able to restore growth on glycerol. Triclosan that is used as an antibacterial agent against fatty acid synthesis type II 2-enoyl thioester reductases inhibited growth of FabI overexpressing mutant yeast cells but was not able to inhibit respiratory growth of the ETR2- or ETR1-complemented mutant yeast cells. Resolving of crystal structures obtained via Etr2p and Etr1p co-crystallization indicated that all possible dimer variants occur in the same asymmetric unit, suggesting that similar dimer formation also takes place in vivo.
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==About this Structure==
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Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers.,Torkko JM, Koivuranta KT, Kastaniotis AJ, Airenne TT, Glumoff T, Ilves M, Hartig A, Gurvitz A, Hiltunen JK J Biol Chem. 2003 Oct 17;278(42):41213-20. Epub 2003 Jul 30. PMID:12890667<ref>PMID:12890667</ref>
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1N9G is a [[Protein complex]] structure of sequences 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=1N9G 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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Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers., Torkko JM, Koivuranta KT, Kastaniotis AJ, Airenne TT, Glumoff T, Ilves M, Hartig A, Gurvitz A, Hiltunen JK, J Biol Chem. 2003 Oct 17;278(42):41213-20. Epub 2003 Jul 30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12890667 12890667]
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</div>
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<div class="pdbe-citations 1n9g" 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: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Airenne, T T.]]
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[[Category: Airenne TT]]
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[[Category: Glumoff, T.]]
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[[Category: Glumoff T]]
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[[Category: Gurvitz, A.]]
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[[Category: Gurvitz A]]
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[[Category: Hartig, A.]]
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[[Category: Hartig A]]
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[[Category: Hiltunen, J K.]]
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[[Category: Hiltunen JK]]
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[[Category: Ilves, M.]]
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[[Category: Ilves M]]
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[[Category: Kastaniotis, A J.]]
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[[Category: Kastaniotis AJ]]
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[[Category: Koivuranta, K T.]]
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[[Category: Koivuranta KT]]
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[[Category: Torkko, J M.]]
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[[Category: Torkko JM]]
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[[Category: Heterodimer]]
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[[Category: Rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 04:51:29 2008''
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Current revision

Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis

PDB ID 1n9g

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