Crystallization and preliminary analysis of the NqrA and NqrC subunits of the Na+‐translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae. Issue 7 (1st July 2014)

• Record Type: Journal Article
• Authors: Vohl, Georg; Nedielkov, Ruslan; Claussen, Björn; Casutt, Marco S.; Vorburger, Thomas; Diederichs, Kay; Möller, Heiko M.; Steuber, Julia; Fritz, Günter
• Is Part Of: Acta crystallographica. Volume 70:Issue 7(2014:Jul.)
• Page Start: 987
• Page End: 992
• Publication Date: 2014-07-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14009881
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The Na⁺‐translocating NADH:ubiquinone oxidoreductase (Na⁺‐NQR) from <italic>Vibrio cholerae</italic> 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 <italic>Escherichia coli</italic> and crystallized. The structure of NqrA_1–377 was solved in space groups <italic>C</italic>222₁ and <italic>P</italic>2₁ 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 <italic>Parabacteroides distasonis</italic> as search model at 1.8 Å resolution.</p> </abstract>