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

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2014

Autor:innen

Vohl, Georg
Claussen, Björn
Casutt, Marco S.
Vorburger, Thomas
Steuber, Julia

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Acta Crystallographica Section F : Structural Biology and Crystallization Communications. 2014, 70(7), pp. 987-992. eISSN 1744-3091. Available under: doi: 10.1107/S2053230X14009881

Zusammenfassung

The 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.

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Fachgebiet (DDC)
570 Biowissenschaften, Biologie

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Vibrio cholerae; Na+-translocating NQR; covalently bound FMN.

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ISO 690VOHL, 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/S2053230X14009881
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}
}
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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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