6SD1

Structure of the RBM3/collar region of the Salmonella flagella MS-ring protein FliF with 33-fold symmetry applied

Summary for 6SD1

• Entry DOI: 10.2210/pdb6sd1/pdb
• Related: 6SCN
• EMDB information: 10143 10145
• Descriptor: Flagellar M-ring protein (1 entity in total)
• Functional Keywords: flagella, secretion, rotor, ms-ring, c-ring, motor protein
• Biological source: Salmonella enterica subsp. enterica serovar 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: 2019-07-26, 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

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: 32284565
DOI: 10.1038/s41564-020-0703-3

Experimental method

ELECTRON MICROSCOPY (2.6 Å)