High resolution structure of the ba3 cytochrome c oxidase from Thermus thermophilus in a lipidic environment.

ABSTRACT: The fundamental chemistry underpinning aerobic life on Earth involves reduction of dioxygen to water with concomitant proton translocation. This process is catalyzed by members of the heme-copper oxidase (HCO) superfamily. Despite the availability of crystal structures for all types of HCO, the mode of action for this enzyme is not understood at the atomic level, namely how vectorial H(+) and e(-) transport are coupled. Toward addressing this problem, we report wild type and A120F mutant structures of the ba(3)-type cytochrome c oxidase from Thermus thermophilus at 1.8 Å resolution. The enzyme has been crystallized from the lipidic cubic phase, which mimics the biological membrane environment. The structures reveal 20 ordered lipid molecules that occupy binding sites on the protein surface

SUBMITTER: Tiefenbrunn T 

PROVIDER: S-EPMC3141039 | biostudies-literature | 2011

REPOSITORIES: biostudies-literature