Structure and function in mitochondrial cristae are shaped by interactions between ATP synthase dimers and cardiolipin lipids, but the underlying mechanisms remain unclear. Here, using molecular dynamics simulations, the authors show that the altered lipid environment in Barth syndrome disrupts cardiolipin interactions at the dimer interface, leading to a reduced wedge angle of the ATP synthase dimer that may compromise crista architecture and OXPHOS efficiency.
- M. Makowski
- V. G. Almendro-Vedia
- I. López-Montero
