Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 70, Issue -, Pages 987-992Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X14009881
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Funding
- Baden-Wurttemberg Stiftung [P-LS-Meth/4]
- Deutsche Forschungsgemeinschaft [FR 1321/3-1, FR 1488/3-2]
- University of Konstanz
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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 angstrom 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 angstrom resolution.
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