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| | <StructureSection load='1n9g' size='340' side='right'caption='[[1n9g]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='1n9g' size='340' side='right'caption='[[1n9g]], [[Resolution|resolution]] 1.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1n9g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_4563 Atcc 4563]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1N9G FirstGlance]. <br> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gu7|1gu7]], [[1guf|1guf]], [[1gyr|1gyr]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ETR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 ATCC 4563]), ETR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 ATCC 4563])</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=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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9g OCA], [http://pdbe.org/1n9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n9g RCSB], [http://www.ebi.ac.uk/pdbsum/1n9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9g ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://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> | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 4563]] | + | [[Category: Candida tropicalis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Airenne, T T]] | + | [[Category: Airenne TT]] |
| - | [[Category: Glumoff, T]] | + | [[Category: Glumoff T]] |
| - | [[Category: Gurvitz, A]] | + | [[Category: Gurvitz A]] |
| - | [[Category: Hartig, A]] | + | [[Category: Hartig A]] |
| - | [[Category: Hiltunen, J K]] | + | [[Category: Hiltunen JK]] |
| - | [[Category: Ilves, M]] | + | [[Category: Ilves M]] |
| - | [[Category: Kastaniotis, A J]] | + | [[Category: Kastaniotis AJ]] |
| - | [[Category: Koivuranta, K T]] | + | [[Category: Koivuranta KT]] |
| - | [[Category: Torkko, J M]] | + | [[Category: Torkko JM]] |
| - | [[Category: Heterodimer]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
ETR2_CANTR Required for respiration and the maintenance of the mitochondrial compartment. May have a role in the mitochondrial synthesis of fatty acids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Torkko JM, Koivuranta KT, Kastaniotis AJ, Airenne TT, Glumoff T, Ilves M, Hartig A, Gurvitz A, Hiltunen JK. Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers. J Biol Chem. 2003 Oct 17;278(42):41213-20. Epub 2003 Jul 30. PMID:12890667 doi:10.1074/jbc.M307664200
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