F<sub>0</sub>-F<sub>1</sub> coupling and symmetry mismatch in ATP synthase resolved in every F<sub>0</sub> rotation step
説明
<jats:title>Abstract</jats:title><jats:p>The F<jats:sub>0</jats:sub>F<jats:sub>1</jats:sub> ATP synthase, essential for cellular energy production, is composed of the F<jats:sub>0</jats:sub> and F<jats:sub>1</jats:sub> rotary motors. While both F<jats:sub>0</jats:sub> and F<jats:sub>1</jats:sub> have pseudo-symmetric structures, their symmetries do not match. How the symmetry mismatch is solved remains elusive due to missing intermediate structures of rotational steps. Here, for ATP synthases with 3- and 10-fold symmetries in F<jats:sub>1</jats:sub> and F<jats:sub>0</jats:sub>, respectively, we uncovered the mechanical couplings between F<jats:sub>0</jats:sub> and F<jats:sub>1</jats:sub> at every 36° rotation step via molecular dynamics simulations and comparison of cryo-electron microscopy structures from three species. We found that the frustration is shared by several elements. The F<jats:sub>1</jats:sub> stator partially rotates relative to the F<jats:sub>0</jats:sub> stator via elastic distortion of the b-subunits. The rotor can be distorted. The c-ring rotary angles can be deviated from symmetric ones. Additionally, the F<jats:sub>1</jats:sub> motor may take non-canonical structures relieving stronger frustration. Together, we provide comprehensive understanding to solve the symmetry mismatch.</jats:p>
収録刊行物
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- bioRxiv [Preprint]
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bioRxiv [Preprint] 2021-11-14
Cold Spring Harbor Laboratory