8A1V

Sodium pumping NADH-quinone oxidoreductase with substrate Q2

8A1V の概要

• エントリーDOI: 10.2210/pdb8a1v/pdb
• EMDBエントリー: 15090
• 分子名称: Na(+)-translocating NADH-quinone reductase subunit A, UBIQUINONE-2, FLAVIN MONONUCLEOTIDE, ... (15 entities in total)
• 機能のキーワード: quinone, 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: 219435.54

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: 2024-10-16)

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

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: 37710014
DOI: 10.1038/s41594-023-01099-0

実験手法

ELECTRON MICROSCOPY (2.73 Å)