Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	An ancestral interaction module promotes oligomerization in divergent mitochondrial ATP synthases.
Journal, issue, pages	Nat Commun, Vol. 13, Issue 1, Page 5989, Year 2022
Publish date	Oct 11, 2022
Authors	Ondřej Gahura / Alexander Mühleip / Carolina Hierro-Yap / Brian Panicucci / Minal Jain / David Hollaus / Martina Slapničková / Alena Zíková / Alexey Amunts /
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 ...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.
External links	Nat Commun / PubMed:36220811 / PubMed Central
Methods	EM (single particle)
Resolution	2.7 - 4.3 Å
Structure data	15559 8ap6 EMDB-15559, PDB-8ap6: Trypanosoma brucei mitochondrial F1Fo ATP synthase dimer Method: EM (single particle) / Resolution: 3.2 Å 15560 8ap7 EMDB-15560, PDB-8ap7: membrane region of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 2.7 Å 15561 8ap8 EMDB-15561, PDB-8ap8: Peripheral stalk of Trypanosoma brucei mitochondrial ATP synthase Method: EM (single particle) / Resolution: 3.7 Å 15562 8ap9 EMDB-15562, PDB-8ap9: rotor of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.7 Å 15563 8apa EMDB-15563, PDB-8apa: rotational state 1a of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.7 Å 15564 8apb EMDB-15564, PDB-8apb: rotational state 1b of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.8 Å 15565 8apc EMDB-15565, PDB-8apc: rotational state 1c of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.5 Å 15566 8apd EMDB-15566, PDB-8apd: rotational state 1d of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.7 Å 15567 8ape EMDB-15567, PDB-8ape: rotational state 1e of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.7 Å 15568 8apf EMDB-15568, PDB-8apf: rotational state 2a of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 4.3 Å 15570 8apg EMDB-15570, PDB-8apg: rotational state 2b of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.5 Å 15571 8aph EMDB-15571, PDB-8aph: rotational state 2c of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.8 Å 15572 8apj EMDB-15572, PDB-8apj: rotational state 2d of Trypanosoma brucei mitochondrial ATP synthase Method: EM (single particle) / Resolution: 3.8 Å 15573 8apk EMDB-15573, PDB-8apk: rotational state 3 of the Trypanosoma brucei mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 3.7 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM / Adenosine triphosphate ChemComp-MG: Unknown entry ChemComp-CDL: CARDIOLIPIN / phospholipidYM / Cardiolipin ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate ChemComp-LMT: DODECYL-BETA-D-MALTOSIDE / detergentYM ChemComp-Q7G: 2-{[(4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranosyl)oxy]methyl}-4-{[(3beta,9beta,14beta,17beta,25R)-spirost-5-en-3-yl]oxy}butyl 4-O-alpha-D-glucopyranosyl-alpha-D-glucopyranoside ChemComp-PEE: 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipidYM / Discrete optimized protein energy ChemComp-PC1: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM / Phosphatidylcholine ChemComp-UTP: URIDINE 5'-TRIPHOSPHATE / UTPYM / Uridine triphosphate ChemComp-HOH: WATER / Water ChemComp-3PE: 1,2-Distearoyl-sn-glycerophosphoethanolamine / phospholipidYM / Phosphatidylethanolamine
Source	trypanosoma brucei brucei (eukaryote)
Keywords	MEMBRANE PROTEIN / ATP synthase / mitochondria