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	Acanthamoeba ATP synthase structure reveals the TCA cycle is tethered to OXPHOS.
Journal, issue, pages	Cell, Vol. 189, Issue 20, Page 6307-66324.e7, Year 2026
Publish date	Oct 1, 2026
Authors	Michelle Y Fry / Bridget E Luce / Jonathan A Stefely / Michael Z Chen / Felicia G Deng / Tiana M Issa / / Sarah E Calvo / John Samuelson / Vamsi K Mootha / Luke H Chao /
PubMed Abstract	Oxidative phosphorylation (OXPHOS) is a key metabolic process that couples redox energy to ATP production. While some core OXPHOS complex subunits are found across all domains of life, many have ...Oxidative phosphorylation (OXPHOS) is a key metabolic process that couples redox energy to ATP production. While some core OXPHOS complex subunits are found across all domains of life, many have diverged or expanded across evolution-as seen in the protozoan pathogen Acanthamoeba castellanii. By integrating cryo-electron microscopy of unenriched mitochondrial lysate with mass spectrometry proteomics, we resolved the structures of endogenous mitochondrial ATP synthase (complex V), Hsp60, and respiratory complex III from Acanthamoeba. We capture Acanthamoeba ATP synthase in an IF1-inhibited state and reveal how Acanthamoeba-specific subunits and extensions stabilize the molecular machine, which includes a β subunit extension that interfaces with the peripheral stalk. Additionally, we characterize an active malate dehydrogenase (MDH) dimer structurally integrated within the ATP synthase peripheral stalk, thus revealing a direct protein tether between OXPHOS and the tricarboxylic acid cycle. Together, these findings provide structural insight into lineage-specific adaptations in Acanthamoeba that may tune protozoan metabolism.
External links	Cell / PubMed:42822427 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	2.33 - 9.63 Å
Structure data	74149 9zfr EMDB-74149, PDB-9zfr: Mitochondrial Hsp60 from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 3.76 Å 74150 9zfs EMDB-74150, PDB-9zfs: CryoEM structure of respiratory complex III intermediate from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 3.65 Å EMDB-74151: Mitochondrial ATP synthase dimer from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 9.63 Å EMDB-74152: A composite map of the mitochondrial ATP synthase monomer from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 4.21 Å 74153 9zft EMDB-74153, PDB-9zft: Mitochondrial ATP synthase monomer from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 4.3 Å 74154 9zfu EMDB-74154, PDB-9zfu: F1 ATPase from Acanthamoeba castellanii Method: EM (single particle) / Resolution: 3.77 Å 74155 9zfv EMDB-74155, PDB-9zfv: Mitochondrial MDH and OSCP in the peripheral stalk of ATP synthase in Acanthamoeba castellanii Method: EM (single particle) / Resolution: 4.21 Å 74156 9zfw EMDB-74156, PDB-9zfw: Membrane region of Acanthamoeba castellanii mitochondrial ATP synthase dimer Method: EM (single particle) / Resolution: 4.23 Å PDB-9zfx: Mitochondrial malate dehydrogenase from Acanthamoeba castellanii Method: X-RAY DIFFRACTION / Resolution: 2.33 Å
Chemicals	ChemComp-HEM: PROTOPORPHYRIN IX CONTAINING FE ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-HOH: WATER
Source	acanthamoeba castellanii (eukaryote)
Keywords	CHAPERONE / mitochondrial Hsp60 / cryoEM / OXIDOREDUCTASE / complex III / OXPHOS / cytochrome bc1 complex / HYDROLASE / complex V / ATP synthase / OXPHOS complex V / malate dehydrogenase / MDH / mitochondrial