Author: Johnson, Steven; Fong, Yu Hang; Deme, Justin C.; Furlong, Emily J.; Kuhlen, Lucas; Lea, Susan M.
Description: 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.
Subject headings: Bacteria; Bacterial Proteins; Bacterial Secretion Systems; Flagella; Membrane Proteins; Models; Molecular; Molecular Motor Proteins; Protein Conformation; Protein Interaction Domains and Motifs; Protein Multimerization; Spores; Bacterial; Structure-Activity Relationship
Publication year: 2020
Journal or book title: Nature Microbiology
Find the full text: https://www.strategian.com/fulltext/Johnson2020.pdf
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Serial number: 3202