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TitleThe cytoplasmic domain of the AAA+ protease FtsH is tilted with respect to the membrane to facilitate substrate entry.
Journal, issue, pagesJ Biol Chem, Vol. 296, Page 100029, Year 2021
Publish dateNov 23, 2020
AuthorsVanessa Carvalho / Irfan Prabudiansyah / Lubomir Kovacik / Mohamed Chami / Roland Kieffer / Ramon van der Valk / Nick de Lange / Andreas Engel / Marie-Eve Aubin-Tam /
PubMed AbstractAAA+ proteases are degradation machines that use ATP hydrolysis to unfold protein substrates and translocate them through a central pore toward a degradation chamber. FtsH, a bacterial membrane- ...AAA+ proteases are degradation machines that use ATP hydrolysis to unfold protein substrates and translocate them through a central pore toward a degradation chamber. FtsH, a bacterial membrane-anchored AAA+ protease, plays a vital role in membrane protein quality control. How substrates reach the FtsH central pore is an open key question that is not resolved by the available atomic structures of cytoplasmic and periplasmic domains. In this work, we used both negative stain TEM and cryo-EM to determine 3D maps of the full-length Aquifex aeolicus FtsH protease. Unexpectedly, we observed that detergent solubilization induces the formation of fully active FtsH dodecamers, which consist of two FtsH hexamers in a single detergent micelle. The striking tilted conformation of the cytosolic domain in the FtsH dodecamer visualized by negative stain TEM suggests a lateral substrate entrance between the membrane and cytosolic domain. Such a substrate path was then resolved in the cryo-EM structure of the FtsH hexamer. By mapping the available structural information and structure predictions for the transmembrane helices to the amino acid sequence we identified a linker of ∼20 residues between the second transmembrane helix and the cytosolic domain. This unique polypeptide appears to be highly flexible and turned out to be essential for proper functioning of FtsH as its deletion fully eliminated the proteolytic activity of FtsH.
External linksJ Biol Chem / PubMed:33154162 / PubMed Central
MethodsEM (single particle)
Resolution6.6 - 20.5 Å
Structure data

EMDB-11161:
FtsH protease from A. aeolicus in C6 symmetry
Method: EM (single particle) / Resolution: 6.6 Å

EMDB-11167:
A. aeolicus FtsH protease resolved without imposed symmetry
Method: EM (single particle) / Resolution: 15.9 Å

EMDB-11169:
S-shaped FtsH dodecamer of A. aeolicus with touching N-terminal domains in LMNG micelle
Method: EM (single particle) / Resolution: 20.5 Å

EMDB-11171:
FtsH dodecamer of A. aeolicus in LMNG micelle, tilted at 90 degrees
Method: EM (single particle) / Resolution: 12.13 Å

EMDB-11200:
S-shaped FtsH dodecamer of A. aeolicus with lamellar-like N-terminal domains in LMNG micelle
Method: EM (single particle) / Resolution: 19.5 Å

EMDB-11201:
S-shaped FtsH dodecamer of A. aeolicus with intertwined N-terminal domains in LMNG micelle
Method: EM (single particle) / Resolution: 17.07 Å

Source
  • Escherichia coli (E. coli)

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