1n9g
From Proteopedia
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|PDB= 1n9g |SIZE=350|CAPTION= <scene name='initialview01'>1n9g</scene>, resolution 1.98Å | |PDB= 1n9g |SIZE=350|CAPTION= <scene name='initialview01'>1n9g</scene>, resolution 1.98Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ETR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 Candida tropicalis]), ETR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 Candida tropicalis]) | |GENE= ETR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 Candida tropicalis]), ETR1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5482 Candida tropicalis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1gu7|1GU7]], [[1guf|1GUF]], [[1gyr|1GYR]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9g OCA], [http://www.ebi.ac.uk/pdbsum/1n9g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n9g RCSB]</span> | ||
}} | }} | ||
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[[Category: Koivuranta, K T.]] | [[Category: Koivuranta, K T.]] | ||
[[Category: Torkko, J M.]] | [[Category: Torkko, J M.]] | ||
| - | [[Category: NAP]] | ||
| - | [[Category: SO4]] | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:27:14 2008'' |
Revision as of 19:27, 30 March 2008
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| , resolution 1.98Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | ETR2 (Candida tropicalis), ETR1 (Candida tropicalis) | ||||||
| Related: | 1GU7, 1GUF, 1GYR
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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