3a5x is a 1 chain structure with sequence from Salmonella typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[FLIC_SALTY] Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Evolutionary Conservation
Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Conformational change of flagellin for polymorphic supercoiling of the flagellar filament.,Maki-Yonekura S, Yonekura K, Namba K Nat Struct Mol Biol. 2010 Apr;17(4):417-22. Epub 2010 Mar 14. PMID:20228803[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Maki-Yonekura S, Yonekura K, Namba K. Conformational change of flagellin for polymorphic supercoiling of the flagellar filament. Nat Struct Mol Biol. 2010 Apr;17(4):417-22. Epub 2010 Mar 14. PMID:20228803 doi:http://dx.doi.org/10.1038/nsmb.1774
