Structural basis for different membrane-binding properties of <em>E. coli</em> anaerobic and human mitochondrial β-oxidation trifunctional enzymes
Sah-Teli, Shiv K.; Pinkas, Matyas; Hynönen, Mikko J.; Butcher, Sarah J.; Wierenga, Rik K.; Novacek, Jiri; Venkatesan, Rajaram (2023-05-15)
Sah-Teli, S. K., Pinkas, M., Hynönen, M. J., Butcher, S. J., Wierenga, R. K., Novacek, J., & Venkatesan, R. (2023). Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes. Structure, 31(7), 812-825.e6. https://doi.org/10.1016/j.str.2023.04.011, Structure, 2023, ISSN 0969-2126, https://doi.org/10.1016/j.str.2023.04.011
© 2023 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (https://doi.org/10.1016/j.str.2023.04.011).
https://creativecommons.org/licenses/by/4.0/
https://urn.fi/URN:NBN:fi-fe2023052948993
Tiivistelmä
Abstract
Facultative anaerobic bacteria such as Escherichia coli have two α₂β₂ heterotetrameric trifunctional enzymes (TFE), catalyzing the last three steps of the β-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-α 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-α result in weaker α-β as well as α-membrane interactions, respectively. The protruding H-H region of anEcTFE-β is therefore more critical for membrane-association. Mutational studies also show that this region is important for the stability of the anEcTFE-β dimer and anEcTFE heterotetramer. The fatty acyl tail binding tunnel of the anEcTFE-α hydratase domain, as in HsTFE-α, is wider than in EcTFE-α, accommodating longer fatty acyl tails, in good agreement with their respective substrate specificities.
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