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Unusual ATP synthase found in sleeping sickness parasite

January 2017. The mitochondrial F1Fo ATP synthase is an essential membrane protein machine that supplies all eukaryotic cells with ATP. The proton-driven rotation of the rotor assembly in the membrane transmits energy to the catalytic F1 head, where ATP is generated by rotary catalysis. A team of scientists at the Max Planck Instutue of Biophysics in Frankfurt determined the in situ structures of ATP synthase dimers from the lethal sleeping sickness parasite Trypanosoma brucei and its free-living relative Euglena gracilis. In both ATP synthases, the catalytic subunits form a threefold pyramid rather than the usual near-sixfold ring. This unexpected finding indicates that the structure of the F1 head, and therefore its catalytic action, is less highly conserved than previously thought, and provides insight into the fundamental mechanism of ATP production in higher organisms. More ...


Werner Kühlbrandt
Max Planck Institute of Biophysics
Frankfurt/Main, Germany


Reference: Mühleip AW, Dewar CE, Schnaufer A, Kühlbrandt W*, Davies KM* (2017) In situ structure of trypanosomal ATP synthase dimer reveals a unique arrangement of catalytic subunits. P Natl Acad Sci USA, published online 17 January 2017. http://dx.doi.org/10.1073/pnas.1612386114


Cluster of Excellence Macromolecular Complexes, Frankfurt am Main, Germany