6t17

Cryo-EM structure of the wild-type flagellar filament of the Firmicute KurthiaCryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia

6t17, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Structural highlights 6t17 is a 44 chain structure with sequence from Kurthia sp. 11kri321. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.8Å Experimental data: Check Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0X9VHV9_9BACL Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.[RuleBase:RU362073] Publication Abstract from PubMed Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament's supercoil. So far, all studied functional filaments are composed of a mixture of L- and R-state flagellin monomers. Here we show in a study of the wild type Firmicute Kurthia sp., that curved, functional filaments can adopt a conformation in vivo that is closely related to a uniform, all-L-state. This sheds additional light on transitions of the flagellar supercoil and uniquely reveals the atomic structure of a wild-type flagellar filament in vivo, including six residues showing clearly densities of O-linked glycosylation. The wild-type flagellar filament of the Firmicute Kurthia at 2.8 A resolution in vivo.,Blum TB, Filippidou S, Fatton M, Junier P, Abrahams JP Sci Rep. 2019 Oct 18;9(1):14948. doi: 10.1038/s41598-019-51440-1. PMID:31628388 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Flagellin 3D structures