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Publication Abstract from PubMed

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.

The series of conformational states adopted by rotorless F(1)-ATPase during its hydrolysis cycle.,Sobti M, Ueno H, Brown SHJ, Noji H, Stewart AG Structure. 2024 Apr 4;32(4):393-399.e3. doi: 10.1016/j.str.2023.12.014. Epub 2024 , Jan 17. PMID:38237595^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.