8VWC

CryoEM Structure of a FtsH Helical Assembly in the Aged State

8VWC の概要

• エントリーDOI: 10.2210/pdb8vwc/pdb
• EMDBエントリー: 43581
• 分子名称: ATP-dependent zinc metalloprotease FtsH, MAGNESIUM ION, ZINC ION, ... (4 entities in total)
• 機能のキーワード: nucleotide binding, protease, cytoplasmic domain, helical assembly, hydrolase
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 52090.73

構造登録者

Li, Y.,Zhu, J.,Zhang, Z.,Wang, F.,Egelman, E.H.,Tezcan, F.A. (登録日: 2024-01-31, 公開日: 2025-01-15, 最終更新日: 2025-06-11)

主引用文献

Li, Y.,Zhu, J.,Zhang, Z.,Wei, J.,Wang, F.,Meisl, G.,Knowles, T.P.J.,Egelman, E.H.,Tezcan, F.A.
Transforming an ATP-dependent enzyme into a dissipative, self-assembling system.
Nat.Chem.Biol., 21:883-893, 2025

PubMed Abstract: Nucleoside triphosphate (NTP)-dependent protein assemblies such as microtubules and actin filaments have inspired the development of diverse chemically fueled molecular machines and active materials but their functional sophistication has yet to be matched by design. Given this challenge, we asked whether it is possible to transform a natural adenosine 5'-triphosphate (ATP)-dependent enzyme into a dissipative self-assembling system, thereby altering the structural and functional mode in which chemical energy is used. Here we report that FtsH (filamentous temperature-sensitive protease H), a hexameric ATPase involved in membrane protein degradation, can be readily engineered to form one-dimensional helical nanotubes. FtsH nanotubes require constant energy input to maintain their integrity and degrade over time with the concomitant hydrolysis of ATP, analogous to natural NTP-dependent cytoskeletal assemblies. Yet, in contrast to natural dissipative systems, ATP hydrolysis is catalyzed by free FtsH protomers and FtsH nanotubes serve to conserve ATP, leading to transient assemblies whose lifetimes can be tuned from days to minutes through the inclusion of external ATPases in solution.

PubMed: 39806067
DOI: 10.1038/s41589-024-01811-1

実験手法

ELECTRON MICROSCOPY (2.6 Å)