Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics.
Günce Göc1,2, Sathish K N Yadav3, George Orriss3
1Turkish Accelerator and Radiation Laboratory, Ankara 06830, Türkiye.
ACS Chemical Biology
|April 7, 2026
Summary
The FtsH protease
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- FtsH is a crucial AAA+ metalloprotease in bacteria and organelles, vital for maintaining cellular homeostasis.
- It functions by degrading misfolded and membrane-associated proteins, a key process for cellular health.
Purpose of the Study:
- To investigate the conformational flexibility of the Escherichia coli FtsH periplasmic domain (FtsH-PD).
- To elucidate the structural basis of FtsH-PD's role in protein degradation and translocation.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was used to determine the structures of FtsH-PD.
- Analysis of high-resolution structures revealed distinct conformational states.
Main Results:
- Two distinct conformational states of FtsH-PD were resolved at 4.9 Å and 7.3 Å.
- A novel rotated-helix conformation involving a 20° clockwise rotation of two alpha helices was identified.
Conclusions:
- Conformational changes occur within the FtsH periplasmic domain, not just the cytosolic domain.
- This flexibility, potentially involving the HflKC complex and lipid-scramblase activity, aids substrate translocation and membrane protein extraction, offering new insights into FtsH degradation mechanisms.
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