+Open data
-Basic information
Entry | Database: PDB / ID: 8a1y | ||||||
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Title | Sodium pumping NADH-quinone oxidoreductase with inhibitor HQNO | ||||||
Components | (Na(+)-translocating NADH-quinone reductase subunit ...) x 6 | ||||||
Keywords | MEMBRANE PROTEIN / quinone / NADH / sodium pump / inhibitor | ||||||
Function / homology | Function and homology information NADH:ubiquinone reductase (Na+-transporting) / Gram-negative-bacterium-type cell wall / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / sodium ion transport / respiratory electron transport chain / transmembrane transport / 2 iron, 2 sulfur cluster binding / FMN binding / flavin adenine dinucleotide binding / electron transfer activity ...NADH:ubiquinone reductase (Na+-transporting) / Gram-negative-bacterium-type cell wall / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / sodium ion transport / respiratory electron transport chain / transmembrane transport / 2 iron, 2 sulfur cluster binding / FMN binding / flavin adenine dinucleotide binding / electron transfer activity / metal ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Vibrio cholerae (bacteria) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å | ||||||
Authors | Hau, J.-L. / Kaltwasser, S. / Vonck, J. / Fritz, G. / Steuber, J. | ||||||
Funding support | Germany, 1items
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Citation | Journal: Nat Struct Mol Biol / Year: 2023 Title: Conformational coupling of redox-driven Na-translocation in Vibrio cholerae NADH:quinone oxidoreductase. Authors: Jann-Louis Hau / Susann Kaltwasser / Valentin Muras / Marco S Casutt / Georg Vohl / Björn Claußen / Wojtek Steffen / Alexander Leitner / Eckhard Bill / George E Cutsail / Serena DeBeer / ...Authors: Jann-Louis Hau / Susann Kaltwasser / Valentin Muras / Marco S Casutt / Georg Vohl / Björn Claußen / Wojtek Steffen / Alexander Leitner / Eckhard Bill / George E Cutsail / Serena DeBeer / Janet Vonck / Julia Steuber / Günter Fritz / 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: ...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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
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PDBx/mmCIF format | 8a1y.cif.gz | 731.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8a1y.ent.gz | 603.6 KB | Display | PDB format |
PDBx/mmJSON format | 8a1y.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8a1y_validation.pdf.gz | 2.1 MB | Display | wwPDB validaton report |
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Full document | 8a1y_full_validation.pdf.gz | 2.1 MB | Display | |
Data in XML | 8a1y_validation.xml.gz | 63 KB | Display | |
Data in CIF | 8a1y_validation.cif.gz | 91.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/8a1y ftp://data.pdbj.org/pub/pdb/validation_reports/a1/8a1y | HTTPS FTP |
-Related structure data
Related structure data | 15093MC 8a1tC 8a1uC 8a1vC 8a1wC 8a1xC 8acwC 8acyC 8ad3C 8ad4C 8ad5C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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-Components
-Na(+)-translocating NADH-quinone reductase subunit ... , 6 types, 6 molecules ABCDEF
#1: Protein | Mass: 51125.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: NqrA with N-terminal his-tag and HRV3C protease cleavage site Source: (gene. exp.) Vibrio cholerae (bacteria) Gene: nqrA, ERS013165_00619, ERS013186_02081, ERS013199_02394, ERS013202_01882, ERS013206_02986, ERS013207_01957 Production host: Vibrio cholerae (bacteria) References: UniProt: A0A655PZA5, NADH:ubiquinone reductase (Na+-transporting) |
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#2: Protein | Mass: 45390.883 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae (bacteria) Gene: nqrB, D6U24_04465, ERS013186_02082, ERS013198_02508, ERS013199_02395, ERS013200_04117, ERS013202_01883, ERS013206_02987, ERS013207_01958, EYB64_17950, F0H40_10090, FLM02_04820, FLM12_12920, FXE67_12105, HPY07_02915 Production host: Vibrio cholerae (bacteria) References: UniProt: A0A085SSI3, NADH:ubiquinone reductase (Na+-transporting) |
#3: Protein | Mass: 27652.270 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Vibrio cholerae (bacteria) Gene: nqrC, BC353_01370, D6U24_04470, ERS013165_00616, ERS013186_02083, ERS013198_02507, ERS013199_02396, ERS013200_04118, ERS013201_01110, ERS013202_01884, ERS013206_02988, ERS013207_01959, F0H40_ ...Gene: nqrC, BC353_01370, D6U24_04470, ERS013165_00616, ERS013186_02083, ERS013198_02507, ERS013199_02396, ERS013200_04118, ERS013201_01110, ERS013202_01884, ERS013206_02988, ERS013207_01959, F0H40_10095, FLM02_04815, FLM12_12915 Production host: Vibrio cholerae (bacteria) References: UniProt: A0A085R7S2, NADH:ubiquinone reductase (Na+-transporting) |
#4: Protein | |