» Articles » PMID: 25005105

Crystallization and Preliminary Analysis of the NqrA and NqrC Subunits of the Na+-translocating NADH:ubiquinone Oxidoreductase from Vibrio Cholerae

Overview
Specialty Chemistry
Date 2014 Jul 10
PMID 25005105
Citations 7
Authors
Affiliations
Soon will be listed here.
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.

Citing Articles

Central Carbon Metabolism, Sodium-Motive Electron Transfer, and Ammonium Formation by the Vaginal Pathogen .

Schleicher L, Herdan S, Fritz G, Trautmann A, Seifert J, Steuber J Int J Mol Sci. 2021; 22(21).

PMID: 34769356 PMC: 8585091. DOI: 10.3390/ijms222111925.


Molecular dynamics modeling of the Vibrio cholera Na-translocating NADH:quinone oxidoreductase NqrB-NqrD subunit interface.

Dibrov A, Mourin M, Dibrov P, Pierce G Mol Cell Biochem. 2021; 477(1):153-165.

PMID: 34626300 PMC: 8755685. DOI: 10.1007/s11010-021-04266-3.


A Sodium-Translocating Module Linking Succinate Production to Formation of Membrane Potential in Prevotella bryantii.

Schleicher L, Trautmann A, Stegmann D, Fritz G, Gatgens J, Bott M Appl Environ Microbiol. 2021; 87(21):e0121121.

PMID: 34469197 PMC: 8516057. DOI: 10.1128/AEM.01211-21.


as Host for Expression of Multisubunit Membrane Protein Complexes.

Schleicher L, Muras V, Claussen B, Pfannstiel J, Blombach B, Dibrov P Front Microbiol. 2018; 9:2537.

PMID: 30410475 PMC: 6209661. DOI: 10.3389/fmicb.2018.02537.


The Membrane-Bound C Subunit of Reductive Dehalogenases: Topology Analysis and Reconstitution of the FMN-Binding Domain of PceC.

Buttet G, Willemin M, Hamelin R, Rupakula A, Maillard J Front Microbiol. 2018; 9:755.

PMID: 29740408 PMC: 5928378. DOI: 10.3389/fmicb.2018.00755.


References
1.
Kelley L, Sternberg M . Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc. 2009; 4(3):363-71. DOI: 10.1038/nprot.2009.2. View

2.
DiMaio F, Echols N, Headd J, Terwilliger T, Adams P, Baker D . Improved low-resolution crystallographic refinement with Phenix and Rosetta. Nat Methods. 2013; 10(11):1102-4. PMC: 4116791. DOI: 10.1038/nmeth.2648. View

3.
Duffy E, Barquera B . Membrane topology mapping of the Na+-pumping NADH: quinone oxidoreductase from Vibrio cholerae by PhoA-green fluorescent protein fusion analysis. J Bacteriol. 2006; 188(24):8343-51. PMC: 1698230. DOI: 10.1128/JB.01383-06. View

4.
Nedielkov R, Steffen W, Steuber J, Moller H . NMR reveals double occupancy of quinone-type ligands in the catalytic quinone binding site of the Na+-translocating NADH:Quinone oxidoreductase from Vibrio cholerae. J Biol Chem. 2013; 288(42):30597-30606. PMC: 3798530. DOI: 10.1074/jbc.M112.435750. View

5.
Bertsova Y, Fadeeva M, Kostyrko V, Serebryakova M, Baykov A, Bogachev A . Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins. J Biol Chem. 2013; 288(20):14276-14286. PMC: 3656284. DOI: 10.1074/jbc.M113.455402. View