8BRJ
Escherichia coli anaerobic fatty acid beta oxidation trifunctional enzyme (anEcTFE) trimeric complex
Summary for 8BRJ
| Entry DOI | 10.2210/pdb8brj/pdb |
| EMDB information | 16217 |
| Descriptor | 3-ketoacyl-CoA thiolase FadI, Fatty acid oxidation complex subunit alpha (2 entities in total) |
| Functional Keywords | complex, heterotrimer, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 3 |
| Total formula weight | 173573.27 |
| Authors | Sah-Teli, S.K.,Pinkas, M.,Novacek, J.,Venkatesan, R. (deposition date: 2022-11-23, release date: 2023-05-17, Last modification date: 2024-07-24) |
| 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 Cited by 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: 37192613DOI: 10.1016/j.str.2023.04.011 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.08 Å) |
Structure validation
Download full validation report
