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@article{2262037,
author = {Gahura, Ondrej and Muhleip, Alexander and HierroandYap, Carolina and Panicucci, Brian and Jain, Minal and Hollaus, David and Slapnickova, Martina and Zikova, Alena and Amunts, Alexey},
article_location = {London},
article_number = {1},
doi = {http://dx.doi.org/10.1038/s41467-022-33588-z},
keywords = {TRYPANOSOMA-BRUCEIMODELDIMERRNAVALIDATIONSOFTWARECOMPLEXCHAIN},
language = {eng},
issn = {2041-1723},
journal = {Nature Communications},
title = {An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases},
url = {https://www.nature.com/articles/s41467-022-33588-z},
volume = {13},
year = {2022}
}
TY - JOUR
ID - 2262037
AU - Gahura, Ondrej - Muhleip, Alexander - Hierro-Yap, Carolina - Panicucci, Brian - Jain, Minal - Hollaus, David - Slapnickova, Martina - Zikova, Alena - Amunts, Alexey
PY - 2022
TI - An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases
JF - Nature Communications
VL - 13
IS - 1
SP - 5989
EP - 5989
PB - Nature Publishing Group
SN - 20411723
KW - TRYPANOSOMA-BRUCEIMODELDIMERRNAVALIDATIONSOFTWARECOMPLEXCHAIN
UR - https://www.nature.com/articles/s41467-022-33588-z
N2 - 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. Mitochondrial ATP synthase assemble into oligomers. Here, authors resolve the structure of trypanosomal ATP synthase, showing that its dimerization is essential for function and evolutionary conserved.
ER -
GAHURA, Ondrej, Alexander MUHLEIP, Carolina HIERRO-YAP, Brian PANICUCCI, Minal JAIN, David HOLLAUS, Martina SLAPNICKOVA, Alena ZIKOVA and Alexey AMUNTS. An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases. \textit{Nature Communications}. London: Nature Publishing Group, 2022, vol.~13, No~1, p.~5989-6001. ISSN~2041-1723. Available from: https://dx.doi.org/10.1038/s41467-022-33588-z.
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