Crystallisation and preliminary structure determination of a NADH: quinone oxidoreductase from the extremophile Acidianus ambivalens

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Abstract

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.

Original languageEnglish
Pages (from-to)842-845
Number of pages4
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1764
Issue number4
DOIs
Publication statusPublished - 1 Apr 2006

Keywords

  • Aerobic respiratory chain
  • Archaea
  • Crystallisation
  • Extremophile
  • Membrane protein
  • NADH:quinone oxidoreductase

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