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

DOI: 10.1107/S2053230X14009881
PMID: 25005105

Authors: Georg Vohl (University of Freiburg) , Ruslan Nedielkov (University of Konstanz) , Björn Claussen (University of Freiburg) , Marco S. Casutt (University of Freiburg) , Thomas Vorburger (University of Hohenheim) , Kay Diederichs (University of Konstanz) , Heiko M. Möller (University of Konstanz) , Julia Steuber (University of Hohenheim) , Guenter Fritz (University of Freiburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 70 (7) , PAGES 987 - 992

State: Published (Approved)
Published: July 2014
Diamond Proposal Number(s): 9694 , 10210

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.

Journal Keywords: Vibrio Cholerae; Membrane Protein

Diamond Keywords: Cholera; Bacteria

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: X06SA, X06DA at Swiss Light Source

Added On: 30/09/2015 23:52

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)