1n9g
From Proteopedia
(New page: 200px<br /><applet load="1n9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n9g, resolution 1.98Å" /> '''Mitochondrial 2-enoy...) |
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| - | [[Image:1n9g.jpg|left|200px]]<br /><applet load="1n9g" size=" | + | [[Image:1n9g.jpg|left|200px]]<br /><applet load="1n9g" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1n9g, resolution 1.98Å" /> | caption="1n9g, resolution 1.98Å" /> | ||
'''Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis'''<br /> | '''Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Here we report on the cloning of a Candida tropicalis gene, ETR2, that is | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1N9G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] with SO4 and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1N9G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Candida_tropicalis Candida tropicalis] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9G OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Candida tropicalis]] | [[Category: Candida tropicalis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Airenne, T | + | [[Category: Airenne, T T.]] |
[[Category: Glumoff, T.]] | [[Category: Glumoff, T.]] | ||
[[Category: Gurvitz, A.]] | [[Category: Gurvitz, A.]] | ||
[[Category: Hartig, A.]] | [[Category: Hartig, A.]] | ||
| - | [[Category: Hiltunen, J | + | [[Category: Hiltunen, J K.]] |
[[Category: Ilves, M.]] | [[Category: Ilves, M.]] | ||
| - | [[Category: Kastaniotis, A | + | [[Category: Kastaniotis, A J.]] |
| - | [[Category: Koivuranta, K | + | [[Category: Koivuranta, K T.]] |
| - | [[Category: Torkko, J | + | [[Category: Torkko, J M.]] |
[[Category: NAP]] | [[Category: NAP]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| Line 27: | Line 27: | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:03:39 2008'' |
Revision as of 12:03, 21 February 2008
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Mitochondrial 2-enoyl thioester reductase Etr1p/Etr2p heterodimer from Candida tropicalis
Overview
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.
About this Structure
1N9G is a Protein complex structure of sequences from Candida tropicalis with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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