Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae

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dc.contributor.authorVohl, Georg
dc.contributor.authorNedielkov, Ruslan
dc.contributor.authorClaussen, Björn
dc.contributor.authorCasutt, Marco S.
dc.contributor.authorVorburger, Thomas
dc.contributor.authorDiederichs, Kay
dc.contributor.authorMöller, Heiko M.
dc.contributor.authorSteuber, Julia
dc.contributor.authorFritz, Günter
dc.date.accessioned2015-02-11T09:04:03Z
dc.date.available2015-02-11T09:04:03Z
dc.date.issued2014eng
dc.description.abstractThe Na+-translocating NADH:ubiquinone oxidoreductase (Na+-NQR) from Vibrio cholerae is a membrane protein complex consisting of six different subunits NqrA-NqrF. The major domains of the NqrA and NqrC subunits were heterologously expressed in Escherichia coli and crystallized. The structure of NqrA1-377 was solved in space groups C2221 and P21 by SAD phasing and molecular replacement at 1.9 and 2.1 Å resolution, respectively. NqrC devoid of the transmembrane helix was co-expressed with ApbE to insert the flavin mononucleotide group covalently attached to Thr225. The structure was determined by molecular replacement using apo-NqrC of Parabacteroides distasonis as search model at 1.8 Å resolution.eng
dc.description.versionpublished
dc.identifier.doi10.1107/S2053230X14009881eng
dc.identifier.ppn445465204
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/29824
dc.language.isoengeng
dc.rightsterms-of-use
dc.rights.urihttps://rightsstatements.org/page/InC/1.0/
dc.subjectVibrio cholerae; Na<sup>+</sup>-translocating NQR; covalently bound FMN.eng
dc.subject.ddc570eng
dc.titleCrystallization and preliminary analysis of the NqrA and NqrC subunits of the Na<sup>+</sup>-translocating NADH:ubiquinone oxidoreductase from Vibrio choleraeeng
dc.typeJOURNAL_ARTICLEeng
dspace.entity.typePublication
kops.citation.bibtex
@article{Vohl2014Cryst-29824,
  year={2014},
  doi={10.1107/S2053230X14009881},
  title={Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na<sup>+</sup>-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae},
  number={7},
  volume={70},
  journal={Acta Crystallographica Section F : Structural Biology and Crystallization Communications},
  pages={987--992},
  author={Vohl, Georg and Nedielkov, Ruslan and Claussen, Björn and Casutt, Marco S. and Vorburger, Thomas and Diederichs, Kay and Möller, Heiko M. and Steuber, Julia and Fritz, Günter}
}
kops.citation.iso690VOHL, Georg, Ruslan NEDIELKOV, Björn CLAUSSEN, Marco S. CASUTT, Thomas VORBURGER, Kay DIEDERICHS, Heiko M. MÖLLER, Julia STEUBER, Günter FRITZ, 2014. Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. In: Acta Crystallographica Section F : Structural Biology and Crystallization Communications. 2014, 70(7), pp. 987-992. eISSN 1744-3091. Available under: doi: 10.1107/S2053230X14009881deu
kops.citation.iso690VOHL, Georg, Ruslan NEDIELKOV, Björn CLAUSSEN, Marco S. CASUTT, Thomas VORBURGER, Kay DIEDERICHS, Heiko M. MÖLLER, Julia STEUBER, Günter FRITZ, 2014. Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. In: Acta Crystallographica Section F : Structural Biology and Crystallization Communications. 2014, 70(7), pp. 987-992. eISSN 1744-3091. Available under: doi: 10.1107/S2053230X14009881eng
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    <dcterms:abstract xml:lang="eng">The Na&lt;sup&gt;+&lt;/sup&gt;-translocating NADH:ubiquinone oxidoreductase (Na&lt;sup&gt;+&lt;/sup&gt;-NQR) from Vibrio cholerae is a membrane protein complex consisting of six different subunits NqrA-NqrF. The major domains of the NqrA and NqrC subunits were heterologously expressed in Escherichia coli and crystallized. The structure of NqrA&lt;sub&gt;1-377&lt;/sub&gt; was solved in space groups C222&lt;sub&gt;1&lt;/sub&gt; and P2&lt;sub&gt;1&lt;/sub&gt; by SAD phasing and molecular replacement at 1.9 and 2.1 Å resolution, respectively. NqrC devoid of the transmembrane helix was co-expressed with ApbE to insert the flavin mononucleotide group covalently attached to Thr225. The structure was determined by molecular replacement using apo-NqrC of Parabacteroides distasonis as search model at 1.8 Å resolution.</dcterms:abstract>
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kops.sourcefield.plainActa Crystallographica Section F : Structural Biology and Crystallization Communications. 2014, 70(7), pp. 987-992. eISSN 1744-3091. Available under: doi: 10.1107/S2053230X14009881eng
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temp.internal.duplicates<p>Keine Dubletten gefunden. Letzte Überprüfung: 19.11.2014 15:56:17</p>deu

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