8APJ

rotational state 2d of Trypanosoma brucei mitochondrial ATP synthase

This is a non-PDB format compatible entry.

Summary for 8APJ

• Entry DOI: 10.2210/pdb8apj/pdb
• EMDB information: 15572
• Descriptor: subunit-e, subunit-i/j, ATPTB6, ... (34 entities in total)
• Functional Keywords: atp synthase, mitochondria, membrane protein
• Biological source: Trypanosoma brucei brucei; More
• Total number of polymer chains: 42
• Total formula weight: 1027780.71

Authors

Muehleip, A.,Gahura, O.,Zikova, A.,Amunts, A. (deposition date: 2022-08-09, release date: 2022-10-26)

Primary citation

Gahura, O.,Muhleip, A.,Hierro-Yap, C.,Panicucci, B.,Jain, M.,Hollaus, D.,Slapnickova, M.,Zikova, A.,Amunts, A.
An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
Nat Commun, 13:5989-5989, 2022

PubMed 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.

PubMed: 36220811
DOI: 10.1038/s41467-022-33588-z

Experimental method

ELECTRON MICROSCOPY (3.8 Å)