Fig. 5: Structure of T. gondii ATP synthase hexamer reveals two lumenal Fo contact sites between neighbouring dimers. | Nature Communications

Fig. 5: Structure of T. gondii ATP synthase hexamer reveals two lumenal Fo contact sites between neighbouring dimers.

From: ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria

Fig. 5

a First contact site is shown on the ATP synthase hexamer composite map viewed from the lumen with central lipid bilayer and surrounding detergent belt (gold). The lumenal regions of the three dimers interact to form a triangular complex (bottom panel). Three copies of the CHCHD protein ATPTG9 form homotypic interactions. b Second contact site is shown from the side view: tilted helix hairpin (H2, H3) of ATPTG11 mediates interactions with ATPTG5, ATPTG8 and ATPTG10, whereas ATPTG6 interacts with ATPTG8.

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