Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in F1–Fo coupling
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
https://www.nature.com/articles/s41594-024-01219-4.pdf
Reference51 articles.
1. Xu, T., Pagadala, V. & Mueller, D. M. Understanding structure, function, and mutations in the mitochondrial ATP synthase. Micro. Cell 2, 105–125 (2015).
2. Srivastava, A. P. et al. High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane. Science 360, 6389 (2018).
3. Walker, J. E. The ATP synthase: the understood, the uncertain and the unknown. Biochem. Soc. Trans. 41, 1–16 (2013).
4. Boyer, P. D. A perspective of the binding change mechanism for ATP synthesis. FASEB J. 3, 2164–2178 (1989).
5. Walker, J. E. & Dickson, V. K. The peripheral stalk of the mitochondrial ATP synthase. Biochim. Biophys. Acta 1757, 286–296 (2006).
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