8A1X
Sodium pumping NADH-quinone oxidoreductase with inhibitor DQA
8A1X の概要
| エントリーDOI | 10.2210/pdb8a1x/pdb |
| EMDBエントリー | 15092 |
| 分子名称 | Na(+)-translocating NADH-quinone reductase subunit A, 1,2-Distearoyl-sn-glycerophosphoethanolamine, FE2/S2 (INORGANIC) CLUSTER, ... (12 entities in total) |
| 機能のキーワード | quinone, nadh, sodium pump, inhibitor, membrane protein |
| 由来する生物種 | Vibrio cholerae 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 216626.49 |
| 構造登録者 | Hau, J.-L.,Kaltwasser, S.,Vonck, J.,Fritz, G.,Steuber, J. (登録日: 2022-06-02, 公開日: 2023-06-14, 最終更新日: 2024-10-23) |
| 主引用文献 | Hau, J.L.,Kaltwasser, S.,Muras, V.,Casutt, M.S.,Vohl, G.,Claussen, B.,Steffen, W.,Leitner, A.,Bill, E.,Cutsail 3rd, G.E.,DeBeer, S.,Vonck, J.,Steuber, J.,Fritz, G. Conformational coupling of redox-driven Na + -translocation in Vibrio cholerae NADH:quinone oxidoreductase. Nat.Struct.Mol.Biol., 30:1686-1694, 2023 Cited by PubMed Abstract: In the respiratory chain, NADH oxidation is coupled to ion translocation across the membrane to build up an electrochemical gradient. In the human pathogen Vibrio cholerae, the sodium-pumping NADH:quinone oxidoreductase (Na-NQR) generates a sodium gradient by a so far unknown mechanism. Here we show that ion pumping in Na-NQR is driven by large conformational changes coupling electron transfer to ion translocation. We have determined a series of cryo-EM and X-ray structures of the Na-NQR that represent snapshots of the catalytic cycle. The six subunits NqrA, B, C, D, E, and F of Na-NQR harbor a unique set of cofactors that shuttle the electrons from NADH twice across the membrane to quinone. The redox state of a unique intramembranous [2Fe-2S] cluster orchestrates the movements of subunit NqrC, which acts as an electron transfer switch. We propose that this switching movement controls the release of Na from a binding site localized in subunit NqrB. PubMed: 37710014DOI: 10.1038/s41594-023-01099-0 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.2 Å) |
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