Sobti, Meghna and Ueno, Hiroshi and Brown, Simon H.J. and Noji, Hiroyuki and Stewart, Alastair G. (2024) The series of conformational states adopted by rotorless F1-ATPase during its hydrolysis cycle. Structure, 32 (4). pp. 393-399.e3. ISSN 09692126
Full text not available from this repository.Abstract
F(1)F(o) ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalytic mechanism and isolated F(1)-ATPase subcomplexes can also hydrolyze ATP to generate rotation of their central gamma rotor subunit. As ATP is hydrolyzed, the F(1)-ATPase cycles through a series of conformational states that mediates unidirectional rotation of the rotor. However, even in the absence of a rotor, the alpha and beta subunits are still able to pass through a series of conformations, akin to those that generate rotation. Here, we use cryoelectron microscopy to establish the structures of these rotorless states. These structures indicate that cooperativity in this system is likely mediated by contacts between the beta subunit lever domains, irrespective of the presence of the gamma rotor subunit. These findings provide insight into how long-range information may be transferred in large biological systems.
| Item Type: | Article |
|---|---|
| Subjects: | R Medicine > R Medicine (General) |
| Depositing User: | Repository Administrator |
| Date Deposited: | 16 Dec 2024 04:11 |
| Last Modified: | 16 Dec 2024 04:11 |
| URI: | https://eprints.victorchang.edu.au/id/eprint/1535 |
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