8a1v: Difference between revisions
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==Sodium pumping NADH-quinone oxidoreductase with substrate Q2== | |||
<StructureSection load='8a1v' size='340' side='right'caption='[[8a1v]], [[Resolution|resolution]] 2.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8a1v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A1V FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.73Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8a1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a1v OCA], [https://pdbe.org/8a1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a1v RCSB], [https://www.ebi.ac.uk/pdbsum/8a1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a1v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/NQRA_VIBC3 NQRA_VIBC3] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.[HAMAP-Rule:MF_00425] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Conformational coupling of redox-driven Na(+)-translocation in Vibrio cholerae NADH:quinone oxidoreductase.,Hau JL, Kaltwasser S, Muras V, Casutt MS, Vohl G, Claussen B, Steffen W, Leitner A, Bill E, Cutsail GE 3rd, DeBeer S, Vonck J, Steuber J, Fritz G Nat Struct Mol Biol. 2023 Nov;30(11):1686-1694. doi: 10.1038/s41594-023-01099-0. , Epub 2023 Sep 14. PMID:37710014<ref>PMID:37710014</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8a1v" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Quinone reductase 3D structures|Quinone reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio cholerae]] | |||
[[Category: Fritz G]] | |||
[[Category: Hau J-L]] | |||
[[Category: Kaltwasser S]] | |||
[[Category: Steuber J]] | |||
[[Category: Vonck J]] | |||
Latest revision as of 12:25, 17 October 2024
Sodium pumping NADH-quinone oxidoreductase with substrate Q2Sodium pumping NADH-quinone oxidoreductase with substrate Q2
Structural highlights
FunctionNQRA_VIBC3 NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.[HAMAP-Rule:MF_00425] Publication Abstract from PubMedIn 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. Conformational coupling of redox-driven Na(+)-translocation in Vibrio cholerae NADH:quinone oxidoreductase.,Hau JL, Kaltwasser S, Muras V, Casutt MS, Vohl G, Claussen B, Steffen W, Leitner A, Bill E, Cutsail GE 3rd, DeBeer S, Vonck J, Steuber J, Fritz G Nat Struct Mol Biol. 2023 Nov;30(11):1686-1694. doi: 10.1038/s41594-023-01099-0. , Epub 2023 Sep 14. PMID:37710014[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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