8SPV
PS3 F1 Rotorless, no ATP
8SPV の概要
エントリーDOI | 10.2210/pdb8spv/pdb |
EMDBエントリー | 40687 40688 40689 |
分子名称 | ATP synthase subunit alpha, ATP synthase subunit beta (2 entities in total) |
機能のキーワード | membrane, atp synthase, electron transport, translocase |
由来する生物種 | Bacillus sp. PS3 詳細 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 310118.35 |
構造登録者 | |
主引用文献 | 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 Cited by 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: 38237595DOI: 10.1016/j.str.2023.12.014 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.06 Å) |
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