An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F22%3A00563704" target="_blank" >RIV/60077344:_____/22:00563704 - isvavai.cz</a>
Alternative codes found
RIV/60076658:12310/22:43905077 RIV/00216224:14740/22:00128731
Result on the web
<a href="https://www.nature.com/articles/s41467-022-33588-z" target="_blank" >https://www.nature.com/articles/s41467-022-33588-z</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-022-33588-z" target="_blank" >10.1038/s41467-022-33588-z</a>

Result language
angličtina
Original language name
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases
Original language description
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.
Czech name
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Czech description
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Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology

Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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