An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases
Identifikátory výsledku
Kód výsledku v 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>
Nalezeny alternativní kódy
RIV/60076658:12310/22:43905077 RIV/00216224:14740/22:00128731
Výsledek na webu
<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>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases
Popis výsledku v původním jazyce
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.
Název v anglickém jazyce
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases
Popis výsledku anglicky
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.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2022
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Nature Communications
ISSN
2041-1723
e-ISSN
2041-1723
Svazek periodika
13
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
GB - Spojené království Velké Británie a Severního Irska
Počet stran výsledku
13
Strana od-do
5989
Kód UT WoS článku
000866124200004
EID výsledku v databázi Scopus
2-s2.0-85139627888