Publikation: Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
URI (zitierfähiger Link)
DOI (zitierfähiger Link)
Internationale Patentnummer
Link zur Lizenz
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
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 Å 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.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
STEUBER, Julia, Georg VOHL, Marco S. CASUTT, Kay DIEDERICHS, Günter FRITZ, 2014. Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase. In: Nature. 2014, 516(7529), pp. 62-67. ISSN 0028-0836. eISSN 1476-4687. Available under: doi: 10.1038/nature14003BibTex
@article{Steuber2014Struc-29488,
year={2014},
doi={10.1038/nature14003},
title={Structure of the V. cholerae Na<sup>+</sup>-pumping NADH:quinone oxidoreductase},
number={7529},
volume={516},
issn={0028-0836},
journal={Nature},
pages={62--67},
author={Steuber, Julia and Vohl, Georg and Casutt, Marco S. and Diederichs, Kay and Fritz, Günter}
}RDF
<rdf:RDF
xmlns:dcterms="http://purl.org/dc/terms/"
xmlns:dc="http://purl.org/dc/elements/1.1/"
xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
xmlns:bibo="http://purl.org/ontology/bibo/"
xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
xmlns:foaf="http://xmlns.com/foaf/0.1/"
xmlns:void="http://rdfs.org/ns/void#"
xmlns:xsd="http://www.w3.org/2001/XMLSchema#" >
<rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29488">
<dc:contributor>Diederichs, Kay</dc:contributor>
<dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/29488/1/Steuber_0-266967.pdf"/>
<dc:language>eng</dc:language>
<dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/>
<dc:contributor>Vohl, Georg</dc:contributor>
<foaf:homepage rdf:resource="http://localhost:8080/"/>
<dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dc:contributor>Steuber, Julia</dc:contributor>
<dc:creator>Steuber, Julia</dc:creator>
<dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-01-12T09:22:14Z</dcterms:available>
<dc:creator>Fritz, Günter</dc:creator>
<dc:creator>Diederichs, Kay</dc:creator>
<dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/29488/1/Steuber_0-266967.pdf"/>
<dcterms:issued>2014</dcterms:issued>
<dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
<dc:contributor>Casutt, Marco S.</dc:contributor>
<dc:creator>Vohl, Georg</dc:creator>
<dc:rights>terms-of-use</dc:rights>
<dc:creator>Casutt, Marco S.</dc:creator>
<dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2015-01-12T09:22:14Z</dc:date>
<bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/29488"/>
<dcterms:title>Structure of the V. cholerae Na<sup>+</sup>-pumping NADH:quinone oxidoreductase</dcterms:title>
<void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
<dcterms:abstract xml:lang="eng">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<sup>+</sup>-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<sup>+</sup>-NQR complex has been available until now. Here we present the crystal structure of the Na<sup>+</sup>-NQR complex at 3.5 Å 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<sup>+</sup>-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na<sup>+</sup> translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na<sup>+</sup> through the observed channel.</dcterms:abstract>
<dc:contributor>Fritz, Günter</dc:contributor>
</rdf:Description>
</rdf:RDF>
