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4u9u

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Revision as of 08:10, 22 March 2023

Crystal structure of NqrF FAD-binding domain from Vibrio cholerae

Structural highlights

4u9u is a 2 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NQRF_VIBCH 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.

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4u9u"

Categories: Large Structures | Vibrio cholerae | Fritz G

@@ Line 3: / Line 3: @@
 <StructureSection load='4u9u' size='340' side='right'caption='[[4u9u]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4u9u]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4U9U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4U9U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4u9u]] is a 2 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=4U9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4U9U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4p6v|4p6v]]</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=4u9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9u OCA], [https://pdbe.org/4u9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4u9u RCSB], [https://www.ebi.ac.uk/pdbsum/4u9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4u9u ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nqrF, VC_2290 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=4u9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4u9u OCA], [http://pdbe.org/4u9u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4u9u RCSB], [http://www.ebi.ac.uk/pdbsum/4u9u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4u9u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/NQRF_VIBCH NQRF_VIBCH]] 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.
+[https://www.uniprot.org/uniprot/NQRF_VIBCH NQRF_VIBCH] 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillo virgola del koch trevisan 1884]]
 [[Category: Large Structures]]
-[[Category: Fritz, G]]
+[[Category: Vibrio cholerae]]
-[[Category: Oxidoreductase]]
+[[Category: Fritz G]]
-[[Category: Sodium translocation]]

4u9u

From Proteopedia

Revision as of 08:10, 22 March 2023

Crystal structure of NqrF FAD-binding domain from Vibrio cholerae

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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