1N9G

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

Summary for 1N9G

• Entry DOI: 10.2210/pdb1n9g/pdb
• Related: 1GU7 1GUF 1GYR
• Descriptor: 2,4-dienoyl-CoA reductase, SULFATE ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total)
• Functional Keywords: heterodimer, rossmann fold, hydrolase
• Biological source: Candida tropicalis; More
• Cellular location: Mitochondrion: Q8WZM4 Q8WZM3
• Total number of polymer chains: 6
• Total formula weight: 255985.80

Authors

Torkko, J.M.,Koivuranta, K.T.,Kastaniotis, A.J.,Airenne, T.T.,Glumoff, T.,Ilves, M.,Hartig, A.,Gurvitz, A.,Hiltunen, J.K. (deposition date: 2002-11-25, release date: 2003-12-09, Last modification date: 2024-12-25)

Primary citation

Torkko, J.M.,Koivuranta, K.T.,Kastaniotis, A.J.,Airenne, T.T.,Glumoff, T.,Ilves, M.,Hartig, A.,Gurvitz, A.,Hiltunen, J.K.
Candida tropicalis expresses two mitochondrial 2-enoyl thioester reductases that are able to form both homodimers and heterodimers.
J.Biol.Chem., 278:41213-41220, 2003

PubMed Abstract: 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.

PubMed: 12890667
DOI: 10.1074/jbc.M307664200

Experimental method

X-RAY DIFFRACTION (1.98 Å)