8ACW

X-ray structure of Na+-NQR from Vibrio cholerae at 3.4 A resolution

Summary for 8ACW

• Entry DOI: 10.2210/pdb8acw/pdb
• EMDB information: 15089
• Descriptor: Na(+)-translocating NADH-quinone reductase subunit A, POTASSIUM ION, LYSINE, ... (13 entities in total)
• Functional Keywords: respiratory complex, nadh ubiquinone oxido reducatase, na+ pump, membrane protein
• Biological source: Vibrio cholerae; More
• Total number of polymer chains: 6
• Total formula weight: 217761.31

Authors

Fritz, G. (deposition date: 2022-07-07, release date: 2023-07-12, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.4 Å)