August 28, 2025: Dr. Stuti Sharma, Stony Brook University
Автор: CryoEM Service Centers
Загружено: 2025-08-29
Просмотров: 143
Описание:
Conformations of the yeast mitochondrial ATP synthase at low pH reveal unique reaction intermediates
Mitochondrial adenosine triphosphate (ATP) synthase utilizes the proton gradient across the inner mitochondrial membrane to synthesize ATP at its catalytic sites. The enzyme consists of a water-soluble catalytic sector and a membrane-integral proton channel coupled by a central rotor and a peripheral stator. Several structural and single molecule studies conducted mostly at neutral or basic pH have outlined the reaction mechanism of the ATP synthase. However, during hypoxia the pH of the mitochondrial matrix becomes slightly acidic and previous studies have reported pH-dependent conformational changes in the enzyme. In this study, we have used single-particle cryo-EM to analyze the conformational ensemble of the yeast (Saccharomyces cerevisiae) ATP synthase at pH 6. Four conformations of the enzyme were identified, of which three are reaction intermediates. Importantly, we identify two unique conformations with nearly identical positions of the central rotor but different catalytic site conformations. These structures provide new insights into the catalytic mechanism of the ATP synthase and highlight elastic coupling between the catalytic and proton translocating domains.
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