Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force
In FOF1 ATP synthase, driven by the proton motive force across the membrane, the FO motor rotates the central rotor and induces conformational changes in the F1 motor, resulting in ATP synthesis. Recently, many near-atomic resolution structural models have been obtained using cryo-electron microscop...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2022-06-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2022.872565/full |
| _version_ | 1818215772744318976 |
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| author | Shintaroh Kubo Shoji Takada |
| author_facet | Shintaroh Kubo Shoji Takada |
| author_sort | Shintaroh Kubo |
| collection | DOAJ |
| description | In FOF1 ATP synthase, driven by the proton motive force across the membrane, the FO motor rotates the central rotor and induces conformational changes in the F1 motor, resulting in ATP synthesis. Recently, many near-atomic resolution structural models have been obtained using cryo-electron microscopy. Despite high resolution, however, static information alone cannot elucidate how and where the protons pass through the FO and how proton passage is coupled to FO rotation. Here, we review theoretical and computational studies based on FO structure models. All-atom molecular dynamics (MD) simulations elucidated changes in the protonation/deprotonation of glutamate—the protein-carrier residue—during rotation and revealed the protonation states that form the “water wire” required for long-range proton hopping. Coarse-grained MD simulations unveiled a free energy surface based on the protonation state and rotational angle of the rotor. Hybrid Monte Carlo and MD simulations showed how proton transfer is coupled to rotation. |
| first_indexed | 2024-12-12T06:41:24Z |
| format | Article |
| id | doaj.art-e4123a55f208451da69bd66464d90a33 |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-12-12T06:41:24Z |
| publishDate | 2022-06-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-e4123a55f208451da69bd66464d90a332022-12-22T00:34:20ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2022-06-011310.3389/fmicb.2022.872565872565Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive ForceShintaroh Kubo0Shoji Takada1Department of Anatomy and Cell Biology, McGill University, Montreal, QC, CanadaDepartment of Biophysics, Graduate School of Science, Kyoto University, Kyoto, JapanIn FOF1 ATP synthase, driven by the proton motive force across the membrane, the FO motor rotates the central rotor and induces conformational changes in the F1 motor, resulting in ATP synthesis. Recently, many near-atomic resolution structural models have been obtained using cryo-electron microscopy. Despite high resolution, however, static information alone cannot elucidate how and where the protons pass through the FO and how proton passage is coupled to FO rotation. Here, we review theoretical and computational studies based on FO structure models. All-atom molecular dynamics (MD) simulations elucidated changes in the protonation/deprotonation of glutamate—the protein-carrier residue—during rotation and revealed the protonation states that form the “water wire” required for long-range proton hopping. Coarse-grained MD simulations unveiled a free energy surface based on the protonation state and rotational angle of the rotor. Hybrid Monte Carlo and MD simulations showed how proton transfer is coupled to rotation.https://www.frontiersin.org/articles/10.3389/fmicb.2022.872565/fullFOF1 ATP synthasesFO motormolecular dynamics simulationscoarse-grained modelMonte Carlo simulations |
| spellingShingle | Shintaroh Kubo Shoji Takada Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force Frontiers in Microbiology FOF1 ATP synthases FO motor molecular dynamics simulations coarse-grained model Monte Carlo simulations |
| title | Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force |
| title_full | Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force |
| title_fullStr | Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force |
| title_full_unstemmed | Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force |
| title_short | Rotational Mechanism of FO Motor in the F-Type ATP Synthase Driven by the Proton Motive Force |
| title_sort | rotational mechanism of fo motor in the f type atp synthase driven by the proton motive force |
| topic | FOF1 ATP synthases FO motor molecular dynamics simulations coarse-grained model Monte Carlo simulations |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2022.872565/full |
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