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

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...

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Published in:Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2014-07, Vol.70 (7), p.987-992
Main Authors: Vohl, Georg, Nedielkov, Ruslan, Claussen, Björn, Casutt, Marco S., Vorburger, Thomas, Diederichs, Kay, Möller, Heiko M., Steuber, Julia, Fritz, Günter
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Cloning, Molecular
covalently bound FMN
Crystallization
Crystallization Communications
Crystallography, X-Ray
Escherichia coli - genetics
Escherichia coli - metabolism
Flavin Mononucleotide - chemistry
Gene Expression
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Na+-translocating NQR
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits - chemistry
Protein Subunits - genetics
Protein Subunits - metabolism
Quinone Reductases - chemistry
Quinone Reductases - genetics
Quinone Reductases - metabolism
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Structural Homology, Protein
Vibrio cholerae
Vibrio cholerae - chemistry
Vibrio cholerae - enzymology
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Summary: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.
ISSN:2053-230X
2053-230X
DOI:10.1107/S2053230X14009881