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| Title | Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state. |
|---|---|
| Journal, issue, pages | Commun Biol, Vol. 5, Issue 1, Page 257, Year 2022 |
| Publish date | Mar 23, 2022 |
 Authors | Wu Liu / Martien Schoonen / Tong Wang / Sean McSweeney / Qun Liu /  |
| PubMed Abstract | AAA+ proteases regulate numerous physiological and cellular processes through tightly regulated proteolytic cleavage of protein substrates driven by ATP hydrolysis. FtsH is the only known family of ...AAA+ proteases regulate numerous physiological and cellular processes through tightly regulated proteolytic cleavage of protein substrates driven by ATP hydrolysis. FtsH is the only known family of membrane-anchored AAA+ proteases essential for membrane protein quality control. Although a spiral staircase rotation mechanism for substrate translocation across the FtsH pore has been proposed, the detailed conformational changes among various states have not been clear due to absence of FtsH structures in these states. We report here the cryo-EM structure for Thermotoga maritima FtsH (TmFtsH) in a fully ADP-bound symmetric state. Comparisons of the ADP-state structure with its apo-state and a substrate-engaged yeast YME1 structure show conformational changes in the ATPase domains, rather than the protease domains. A reconstruction of the full-length TmFtsH provides structural insights for the dynamic transmembrane and the periplasmic domains. Our structural analyses expand the understanding of conformational switches between different nucleotide states in ATP hydrolysis by FtsH. |
 External links | Commun Biol / PubMed:35322207 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.15 Å |
| Structure data | EMDB-25837, PDB-7tdo: |
| Chemicals |  ChemComp-ADP: |
| Source |
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 Keywords | HYDROLASE / AAA+ ATPase / protease / hexamer / ADP-bound state |
thermotoga maritima (bacteria)