NADH:quinone oxidoreductases (NDHs), constitute one of the electron entry points into membrane-bound respiratory chains, oxidising NADH and reducing quinones. Type-II NDHs (NDH-2) are functionally unable to translocate protons and are typically constituted by a single ∼50 kDa subunit lacking iron-sulfur clusters and containing one flavin as the sole redox centre. No three dimensional crystal structure is yet available for NDHs. We describe the crystallisation and preliminary structure determination of a NDH-2 that contains a covalently bound FAD, isolated from the membrane fraction of Acidianus ambivalens, a hyperthermoacidophilic archaeon capable of growing at 80 °C and pH 2.0. NDH-2 was solubilised with the detergent n-dodecyl-β-d-maltoside and crystallised using ammonium phosphate as precipitant. The structure was solved by MIRAS using Pt and I derivatives.
|Number of pages||4|
|Journal||Biochimica et Biophysica Acta - Proteins and Proteomics|
|Publication status||Published - 1 Apr 2006|
- Aerobic respiratory chain
- Membrane protein
- NADH:quinone oxidoreductase