7VHP
Structural insights into the membrane microdomain organization by SPFH family proteins
Summary for 7VHP
| Entry DOI | 10.2210/pdb7vhp/pdb |
| EMDB information | 32002 |
| Descriptor | ATP-dependent zinc metalloprotease FtsH, Protein HflK, Modulator of FtsH protease HflC (3 entities in total) |
| Functional Keywords | membrane microdomain organization, membrane protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 48 |
| Total formula weight | 2698760.90 |
| Authors | Ma, C.Y.,Wang, C.K.,Luo, D.Y.,Yan, L.,Yang, W.X.,Li, N.N.,Gao, N. (deposition date: 2021-09-22, release date: 2022-03-23, Last modification date: 2024-06-19) |
| Primary citation | Ma, C.,Wang, C.,Luo, D.,Yan, L.,Yang, W.,Li, N.,Gao, N. Structural insights into the membrane microdomain organization by SPFH family proteins. Cell Res., 32:176-189, 2022 Cited by PubMed Abstract: The lateral segregation of membrane constituents into functional microdomains, conceptually known as lipid raft, is a universal organization principle for cellular membranes in both prokaryotes and eukaryotes. The widespread Stomatin, Prohibitin, Flotillin, and HflK/C (SPFH) family proteins are enriched in functional membrane microdomains at various subcellular locations, and therefore were hypothesized to play a scaffolding role in microdomain formation. In addition, many SPFH proteins are also implicated in highly specific processes occurring on the membrane. However, none of these functions is understood at the molecular level. Here we report the structure of a supramolecular complex that is isolated from bacterial membrane microdomains and contains two SPFH proteins (HflK and HflC) and a membrane-anchored AAA+ protease FtsH. HflK and HflC form a circular 24-mer assembly, featuring a laterally segregated membrane microdomain (20 nm in diameter) bordered by transmembrane domains of HflK/C and a completely sealed periplasmic vault. Four FtsH hexamers are embedded inside this microdomain through interactions with the inner surface of the vault. These observations provide a mechanistic explanation for the role of HflK/C and their mitochondrial homologs prohibitins in regulating membrane-bound AAA+ proteases, and suggest a general model for the organization and functionalization of membrane microdomains by SPFH proteins. PubMed: 34975153DOI: 10.1038/s41422-021-00598-3 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.27 Å) |
Structure validation
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