| Literature DB >> 25005105 |
Georg Vohl1, Ruslan Nedielkov2, Björn Claussen3, Marco S Casutt1, Thomas Vorburger4, Kay Diederichs2, Heiko M Möller2, Julia Steuber4, Günter Fritz1.
Abstract
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.Entities:
Keywords: Na+-translocating NQR; Vibrio cholerae; covalently bound FMN
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Year: 2014 PMID: 25005105 PMCID: PMC4089548 DOI: 10.1107/S2053230X14009881
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056