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-Structure paper
タイトル | Structural basis for different membrane-binding properties of E. coli anaerobic and human mitochondrial β-oxidation trifunctional enzymes. |
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ジャーナル・号・ページ | Structure, Vol. 31, Issue 7, Page 812-825.e6, Year 2023 |
掲載日 | 2023年7月6日 |
著者 | Shiv K Sah-Teli / Matyas Pinkas / Mikko J Hynönen / Sarah J Butcher / Rik K Wierenga / Jiri Novacek / Rajaram Venkatesan / |
PubMed 要旨 | 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 ...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. |
リンク | Structure / PubMed:37192613 |
手法 | EM (単粒子) |
解像度 | 3.55 - 10.3 Å |
構造データ | EMDB-16134, PDB-8bnr: EMDB-16135, PDB-8bnu: EMDB-16217, PDB-8brj: |
由来 |
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キーワード | MEMBRANE PROTEIN (膜タンパク質) / complex / heterooctamer / heterotetramer / heterotrimer |