8SPV

PS3 F1 Rotorless, no ATP

Summary for 8SPV

• Entry DOI: 10.2210/pdb8spv/pdb
• EMDB information: 40687 40688 40689
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta (2 entities in total)
• Functional Keywords: membrane, atp synthase, electron transport, translocase
• Biological source: Bacillus sp. PS3; More
• Total number of polymer chains: 6
• Total formula weight: 310118.35

Authors

Sobti, M.,Stewart, A.G. (deposition date: 2023-05-03, release date: 2024-01-24, Last modification date: 2024-04-17)

Primary citation

Sobti, M.,Ueno, H.,Brown, S.H.J.,Noji, H.,Stewart, A.G.
The series of conformational states adopted by rotorless F 1 -ATPase during its hydrolysis cycle.
Structure, 32:393-, 2024

PubMed Abstract: FF ATP synthase interchanges phosphate transfer energy and proton motive force via a rotary catalytic mechanism and isolated F-ATPase subcomplexes can also hydrolyze ATP to generate rotation of their central γ rotor subunit. As ATP is hydrolyzed, the F-ATPase cycles through a series of conformational states that mediates unidirectional rotation of the rotor. However, even in the absence of a rotor, the α and β 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 β subunit lever domains, irrespective of the presence of the γ rotor subunit. These findings provide insight into how long-range information may be transferred in large biological systems.

PubMed: 38237595
DOI: 10.1016/j.str.2023.12.014

Experimental method

ELECTRON MICROSCOPY (3.06 Å)