ATP Synthase - Springer Nature

An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases

We examine cryo-EM diagrams of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. A chain of five ordered water molecules leads to a Proton transfer in the lumenal half-channel. Although overall dimer architecture is varies among eukaryotes, we find that subunit-g and subunit-e together with subunit-e form an ancestral oligomerization motif that is shared between the trypanosomal and mammalian lineages. Therefore, our results show that the subunit-g/e module is a structural component that determines ATP synthase oligomeric assemblies.

Source link: https://doi.org/10.1038/s41467-022-33588-z

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