{"entity": "publication", "iuid": "0078ae699e004afeb6a07fe251e631ba", "timestamp": "2026-08-22T06:56:35.038Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/0078ae699e004afeb6a07fe251e631ba.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/0078ae699e004afeb6a07fe251e631ba"}}, "title": "An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.", "authors": [{"family": "Gahura", "given": "Ond\u0159ej", "initials": "O", "orcid": "0000-0002-2925-4763", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/daf24cfbc3f641e5bad5a18318959313.json"}}, {"family": "M\u00fchleip", "given": "Alexander", "initials": "A", "orcid": "0000-0002-1877-2282", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/391856cb1a4e4a59b2a608701e4153ef.json"}}, {"family": "Hierro-Yap", "given": "Carolina", "initials": "C"}, {"family": "Panicucci", "given": "Brian", "initials": "B"}, {"family": "Jain", "given": "Minal", "initials": "M"}, {"family": "Hollaus", "given": "David", "initials": "D", "orcid": "0000-0001-7403-6434", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/03065685ec1648db85f1ed0aefb23685.json"}}, {"family": "Slapni\u010dkov\u00e1", "given": "Martina", "initials": "M"}, {"family": "Z\u00edkov\u00e1", "given": "Alena", "initials": "A", "orcid": "0000-0002-8686-0225", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a2e3474a7a5c4610aa173be42841388e.json"}}, {"family": "Amunts", "given": "Alexey", "initials": "A", "orcid": "0000-0002-5302-1740", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6c79bee23e114906bc847dfbd0975139.json"}}], "type": "journal article", "published": "2022-10-11", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "13", "issue": "1", "pages": "5989", "issn-l": "2041-1723"}, "abstract": "Mitochondrial ATP synthase forms stable dimers arranged into oligomeric assemblies that generate the inner-membrane curvature essential for efficient energy conversion. Here, we report cryo-EM structures of the intact ATP synthase dimer from Trypanosoma brucei in ten different rotational states. The model consists of 25 subunits, including nine lineage-specific, as well as 36 lipids. The rotary mechanism is influenced by the divergent peripheral stalk, conferring a greater conformational flexibility. Proton transfer in the lumenal half-channel occurs via a chain of five ordered water molecules. The dimerization interface is formed by subunit-g that is critical for interactions but not for the catalytic activity. Although overall dimer architecture varies among eukaryotes, we find that subunit-g together with subunit-e form an ancestral oligomerization motif, which is shared between the trypanosomal and mammalian lineages. Therefore, our data defines the subunit-g/e module as a structural component determining ATP synthase oligomeric assemblies.", "doi": "10.1038/s41467-022-33588-z", "pmid": "36220811", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC9553925"}, {"db": "pii", "key": "10.1038/s41467-022-33588-z"}], "notes": [], "created": "2026-08-21T11:49:08.613Z", "modified": "2026-08-21T11:49:08.781Z"}