Acanthamoeba ATP synthase structure reveals the TCA cycle is tethered to OXPHOS.

Acanthamoeba ATP synthase structure shows a direct protein tether linking the TCA cycle to OXPHOS, revealing a unique metabolic adaptation.

• Why it matters: Understanding how protozoans like Acanthamoeba adapt their energy production pathways can shed light on their metabolic regulation and potential vulnerabilities, which are not well understood.
• What they did: Using cryo-electron microscopy and proteomics, researchers resolved the structures of mitochondrial ATP synthase, Hsp60, and complex III, identifying lineage-specific subunits and an active malate dehydrogenase (MDH) dimer integrated within ATP synthase.
• The result: The discovery of the MDH dimer tethered to ATP synthase suggests a direct physical link between the TCA cycle and oxidative phosphorylation, providing insights into protozoan metabolic tuning and evolution.