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-Structure paper
タイトル | Structure of respiratory complex I reconstituted into lipid nanodiscs reveals an uncoupled conformation. |
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ジャーナル・号・ページ | Elife, Vol. 10, Year 2021 |
掲載日 | 2021年7月26日 |
著者 | Piotr Kolata / Rouslan G Efremov / |
PubMed 要旨 | Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against transmembrane potential. Complex I ...Respiratory complex I is a multi-subunit membrane protein complex that reversibly couples NADH oxidation and ubiquinone reduction with proton translocation against transmembrane potential. Complex I from is among the best functionally characterized complexes, but its structure remains unknown, hindering further studies to understand the enzyme coupling mechanism. Here, we describe the single particle cryo-electron microscopy (cryo-EM) structure of the entire catalytically active complex I reconstituted into lipid nanodiscs. The structure of this mesophilic bacterial complex I displays highly dynamic connection between the peripheral and membrane domains. The peripheral domain assembly is stabilized by unique terminal extensions and an insertion loop. The membrane domain structure reveals novel dynamic features. Unusual conformation of the conserved interface between the peripheral and membrane domains suggests an uncoupled conformation of the complex. Considering constraints imposed by the structural data, we suggest a new simple hypothetical coupling mechanism for the molecular machine. |
リンク | Elife / PubMed:34308841 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.1 - 6.7 Å |
構造データ | EMDB-12652, PDB-7nyh: EMDB-12653, PDB-7nyr: EMDB-12654, PDB-7nyu: EMDB-12655, PDB-7nyv: EMDB-12661, PDB-7nz1: EMDB-13291: |
化合物 | ChemComp-SF4: ChemComp-FES: ChemComp-FMN: ChemComp-CA: ChemComp-HOH: |
由来 |
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キーワード | ELECTRON TRANSPORT / NADH:ubiquinone reductase (H+-translocating) / oxidative phosphorylation |