7TDO

Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state

Summary for 7TDO

• Entry DOI: 10.2210/pdb7tdo/pdb
• EMDB information: 25837
• Descriptor: ATP-dependent zinc metalloprotease FtsH, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• Functional Keywords: aaa+ atpase, protease, hexamer, adp-bound state, hydrolase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 6
• Total formula weight: 413501.19

Authors

Liu, W.,Schoonen, M.,Wang, T.,McSweeney, S.,Liu, Q. (deposition date: 2022-01-02, release date: 2022-04-06, Last modification date: 2024-02-28)

Primary citation

Liu, W.,Schoonen, M.,Wang, T.,McSweeney, S.,Liu, Q.
Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state.
Commun Biol, 5:257-257, 2022

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 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.

PubMed: 35322207
DOI: 10.1038/s42003-022-03213-2

Experimental method

ELECTRON MICROSCOPY (3.15 Å)