8VW9
CryoEM Structure of a FtsH Helical Assembly in the Presence of ATP
Summary for 8VW9
| Entry DOI | 10.2210/pdb8vw9/pdb |
| EMDB information | 43577 |
| Descriptor | ATP-dependent zinc metalloprotease FtsH, MAGNESIUM ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | nucleotide binding, protease, cytoplasmic domain, helical assembly, hydrolase |
| Biological source | Thermotoga maritima |
| Total number of polymer chains | 1 |
| Total formula weight | 52090.73 |
| Authors | Li, Y.,Zhu, J.,Zhang, Z.,Wang, F.,Egelman, E.H.,Tezcan, F.A. (deposition date: 2024-01-31, release date: 2025-01-15, Last modification date: 2025-01-29) |
| Primary citation | 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., 2025 Cited by 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: 39806067DOI: 10.1038/s41589-024-01811-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.6 Å) |
Structure validation
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