9CZ2
Cryo-EM structure of a nautilus-like HflK/C assembly in complex with FtsH AAA protease
This is a non-PDB format compatible entry.
Summary for 9CZ2
| Entry DOI | 10.2210/pdb9cz2/pdb |
| EMDB information | 46057 |
| Descriptor | Modulator of FtsH protease HflK, Modulator of FtsH protease HflC, ATP-dependent zinc metalloprotease FtsH (3 entities in total) |
| Functional Keywords | ftsh, hflk, hflc, aaa protease, chaperone |
| Biological source | Escherichia coli BL21 More |
| Total number of polymer chains | 36 |
| Total formula weight | 1849196.53 |
| Authors | Ghanbarpour, A.,Sauer, R.T.,Davis, J.H. (deposition date: 2024-08-03, release date: 2024-11-13, Last modification date: 2025-05-28) |
| Primary citation | Ghanbarpour, A.,Telusma, B.,Powell, B.M.,Zhang, J.J.,Bolstad, I.,Vargas, C.,Keller, S.,Baker, T.A.,Sauer, R.T.,Davis, J.H. An asymmetric nautilus-like HflK/C assembly controls FtsH proteolysis of membrane proteins. Embo J., 44:2501-2513, 2025 Cited by PubMed Abstract: The AAA protease FtsH associates with HflK/C subunits to form a megadalton-size complex that spans the inner membrane and extends into the periplasm of E. coli. How this bacterial complex and homologous assemblies in eukaryotic organelles recruit, extract, and degrade membrane-embedded substrates is unclear. Following the overproduction of protein components, recent cryo-EM structures showed symmetric HflK/C cages surrounding FtsH in a manner proposed to inhibit the degradation of membrane-embedded substrates. Here, we present structures of native protein complexes, in which HflK/C instead forms an asymmetric nautilus-shaped assembly with an entryway for membrane-embedded substrates to reach and be engaged by FtsH. Consistent with this nautilus-like structure, proteomic assays suggest that HflK/C enhances FtsH degradation of certain membrane-embedded substrates. Membrane curvature in our FtsH•HflK/C complexes is opposite that of surrounding membrane regions, a property that correlates with lipid scramblase activity and possibly with FtsH's function in the degradation of membrane-embedded proteins. PubMed: 40082723DOI: 10.1038/s44318-025-00408-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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