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| | ==Crystal structure of NqrF in hexagonal space group== | | ==Crystal structure of NqrF in hexagonal space group== |
| - | <StructureSection load='4uaj' size='340' side='right' caption='[[4uaj]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='4uaj' size='340' side='right'caption='[[4uaj]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4uaj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UAJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UAJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4uaj]] is a 1 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=4UAJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UAJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7019Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u9u|4u9u]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uaj OCA], [http://pdbe.org/4uaj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uaj RCSB], [http://www.ebi.ac.uk/pdbsum/4uaj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uaj ProSAT]</span></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=4uaj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uaj OCA], [https://pdbe.org/4uaj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uaj RCSB], [https://www.ebi.ac.uk/pdbsum/4uaj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uaj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/NQRF_VIBC3 NQRF_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. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.[HAMAP-Rule:MF_00430] | + | [https://www.uniprot.org/uniprot/NQRF_VIBC3 NQRF_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. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.[HAMAP-Rule:MF_00430] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fritz, G]] | + | [[Category: Large Structures]] |
| - | [[Category: Nqr]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Sodium translocation]]
| + | |
| | [[Category: Vibrio cholerae]] | | [[Category: Vibrio cholerae]] |
| | + | [[Category: Fritz G]] |
| Structural highlights
Function
NQRF_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. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.[HAMAP-Rule:MF_00430]
Publication Abstract from PubMed
NADH oxidation in the respiratory chain is coupled to ion translocation across the membrane to build up an electrochemical gradient. The sodium-translocating NADH:quinone oxidoreductase (Na(+)-NQR), a membrane protein complex widespread among pathogenic bacteria, consists of six subunits, NqrA, B, C, D, E and F. To our knowledge, no structural information on the Na(+)-NQR complex has been available until now. Here we present the crystal structure of the Na(+)-NQR complex at 3.5 A resolution. The arrangement of cofactors both at the cytoplasmic and the periplasmic side of the complex, together with a hitherto unknown iron centre in the midst of the membrane-embedded part, reveals an electron transfer pathway from the NADH-oxidizing cytoplasmic NqrF subunit across the membrane to the periplasmic NqrC, and back to the quinone reduction site on NqrA located in the cytoplasm. A sodium channel was localized in subunit NqrB, which represents the largest membrane subunit of the Na(+)-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na(+) translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na(+) through the observed channel.
Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase.,Steuber J, Vohl G, Casutt MS, Vorburger T, Diederichs K, Fritz G Nature. 2014 Dec 4;516(7529):62-7. doi: 10.1038/nature14003. PMID:25471880[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Steuber J, Vohl G, Casutt MS, Vorburger T, Diederichs K, Fritz G. Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase. Nature. 2014 Dec 4;516(7529):62-7. doi: 10.1038/nature14003. PMID:25471880 doi:http://dx.doi.org/10.1038/nature14003
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