Structural highlights
Function
FADI_ECOLI Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids.[1] [2]
Publication Abstract from PubMed
Facultative anaerobic bacteria such as Escherichia coli have two alpha(2)beta(2) heterotetrameric trifunctional enzymes (TFE), catalyzing the last three steps of the beta-oxidation cycle: soluble aerobic TFE (EcTFE) and membrane-associated anaerobic TFE (anEcTFE), closely related to the human mitochondrial TFE (HsTFE). The cryo-EM structure of anEcTFE and crystal structures of anEcTFE-alpha show that the overall assembly of anEcTFE and HsTFE is similar. However, their membrane-binding properties differ considerably. The shorter A5-H7 and H8 regions of anEcTFE-alpha result in weaker alpha-beta as well as alpha-membrane interactions, respectively. The protruding H-H region of anEcTFE-beta is therefore more critical for membrane-association. Mutational studies also show that this region is important for the stability of the anEcTFE-beta dimer and anEcTFE heterotetramer. The fatty acyl tail binding tunnel of the anEcTFE-alpha hydratase domain, as in HsTFE-alpha, is wider than in EcTFE-alpha, accommodating longer fatty acyl tails, in good agreement with their respective substrate specificities.
Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial beta-oxidation trifunctional enzymes.,Sah-Teli SK, Pinkas M, Hynonen MJ, Butcher SJ, Wierenga RK, Novacek J, Venkatesan R Structure. 2023 Jul 6;31(7):812-825.e6. doi: 10.1016/j.str.2023.04.011. Epub 2023 , May 15. PMID:37192613[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Snell KD, Feng F, Zhong L, Martin D, Madison LL. YfcX enables medium-chain-length poly(3-hydroxyalkanoate) formation from fatty acids in recombinant Escherichia coli fadB strains. J Bacteriol. 2002 Oct;184(20):5696-705. PMID:12270828 doi:10.1128/JB.184.20.5696-5705.2002
- ↑ Campbell JW, Morgan-Kiss RM, Cronan JE Jr. A new Escherichia coli metabolic competency: growth on fatty acids by a novel anaerobic beta-oxidation pathway. Mol Microbiol. 2003 Feb;47(3):793-805. doi: 10.1046/j.1365-2958.2003.03341.x. PMID:12535077 doi:http://dx.doi.org/10.1046/j.1365-2958.2003.03341.x
- ↑ Sah-Teli SK, Pinkas M, Hynönen MJ, Butcher SJ, Wierenga RK, Novacek J, Venkatesan R. Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes. Structure. 2023 Jul 6;31(7):812-825.e6. PMID:37192613 doi:10.1016/j.str.2023.04.011
