8BNR

Escherichia coli anaerobic fatty acid beta oxidation trifunctional enzyme (anEcTFE) octameric complex

This is a non-PDB format compatible entry.

Summary for 8BNR

• Entry DOI: 10.2210/pdb8bnr/pdb
• EMDB information: 16134
• Descriptor: 3-ketoacyl-CoA thiolase FadI, Fatty acid oxidation complex subunit alpha (2 entities in total)
• Functional Keywords: complex, heterooctamer, membrane protein
• Biological source: Escherichia coli K-12; More
• Total number of polymer chains: 8
• Total formula weight: 501484.78

Authors

Sah-Teli, S.K.,Pinkas, M.,Novacek, J.,Venkatesan, R. (deposition date: 2022-11-14, release date: 2023-05-17, Last modification date: 2023-11-29)

Primary citation

Sah-Teli, S.K.,Pinkas, M.,Hynonen, M.J.,Butcher, S.J.,Wierenga, R.K.,Novacek, J.,Venkatesan, R.
Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial beta-oxidation trifunctional enzymes.
Structure, 31:812-, 2023

PubMed Abstract: Facultative anaerobic bacteria such as Escherichia coli have two αβ 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.

PubMed: 37192613
DOI: 10.1016/j.str.2023.04.011

Experimental method

ELECTRON MICROSCOPY (10.3 Å)