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-Structure paper
Title | Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation. |
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Journal, issue, pages | Nat Microbiol, Vol. 5, Issue 7, Page 966-975, Year 2020 |
Publish date | Apr 13, 2020 |
Authors | Steven Johnson / Yu Hang Fong / Justin C Deme / Emily J Furlong / Lucas Kuhlen / Susan M Lea / |
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 ...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. |
External links | Nat Microbiol / PubMed:32284565 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.6 - 4.5 Å |
Structure data | EMDB-10143, PDB-6scn: EMDB-10145, PDB-6sd1: EMDB-10146, PDB-6sd2: EMDB-10147, PDB-6sd3: EMDB-10148, PDB-6sd4: EMDB-10149, PDB-6sd5: EMDB-10560, PDB-6tre: EMDB-10561: |
Source |
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Keywords | MOTOR PROTEIN / Flagella / Secretion / Rotor / MS-ring / C-ring / T3SS |