3A5X

Conformational change of flagellin for polymorphic supercoiling of the flagellar filament

(2010) Nat Struct Mol Biol 17: 417-422

• PubMed: 20228803 Search on PubMed
• DOI: https://doi.org/10.1038/nsmb.1774
• Primary Citation of Related Structures:  
  3A5X


• PubMed Abstract: 
  

  The bacterial flagellar filament is a helical propeller rotated by the flagellar motor for bacterial locomotion. The filament is a supercoiled assembly of a single protein, flagellin, and is formed by 11 protofilaments. For bacterial taxis, the reversal of motor rotation switches the supercoil between left- and right-handed, both of which arise from combinations of two distinct conformations and packing interactions of the L-type and R-type protofilaments. Here we report an atomic model of the L-type straight filament by electron cryomicroscopy and helical image analysis. Comparison with the R-type structure shows interesting features: an orientation change of the outer core domains (D1) against the inner core domains (D0) showing almost invariant orientation and packing, a conformational switching within domain D1, and the conformational flexibility of domains D0 and D1 with their spoke-like connection for tight molecular packing.

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Organizational Affiliation: 

Dynamic NanoMachine Project, International Cooperative Research Project, Japan Science and Technology Agency, Suita, Osaka, Japan.