6SCN
33mer structure of the Salmonella flagella MS-ring protein FliF
Summary for 6SCN
Entry DOI | 10.2210/pdb6scn/pdb |
EMDB information | 10143 |
Descriptor | Flagellar M-ring protein (1 entity in total) |
Functional Keywords | flagella, secretion, rotor, ms-ring, c-ring, motor protein |
Biological source | Salmonella typhimurium |
Total number of polymer chains | 33 |
Total formula weight | 2022756.28 |
Authors | Johnson, S.,Fong, Y.H.,Deme, J.C.,Furlong, E.J.,Kuhlen, L.,Lea, S.M. (deposition date: 2019-07-24, release date: 2020-03-18, Last modification date: 2024-05-22) |
Primary citation | Johnson, S.,Fong, Y.H.,Deme, J.C.,Furlong, E.J.,Kuhlen, L.,Lea, S.M. Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation. Nat Microbiol, 5:966-975, 2020 Cited by PubMed Abstract: The bacterial flagellum is a complex self-assembling nanomachine that confers motility to the cell. Despite great variation across species, all flagella are ultimately constructed from a helical propeller that is attached to a motor embedded in the inner membrane. The motor consists of a series of stator units surrounding a central rotor made up of two ring complexes, the MS-ring and the C-ring. Despite many studies, high-resolution structural information is still lacking for the MS-ring of the rotor, and proposed mismatches in stoichiometry between the two rings have long provided a source of confusion for the field. Here, we present structures of the Salmonella MS-ring, revealing a high level of variation in inter- and intrachain symmetry that provides a structural explanation for the ability of the MS-ring to function as a complex and elegant interface between the two main functions of the flagellum-protein secretion and rotation. PubMed: 32284565DOI: 10.1038/s41564-020-0703-3 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
Download full validation report