7SQD

Cryo-EM structure of the Achromobacter flagellar filament

This is a non-PDB format compatible entry.

Summary for 7SQD

• Entry DOI: 10.2210/pdb7sqd/pdb
• EMDB information: 25382
• Descriptor: Flagellin (1 entity in total)
• Functional Keywords: bacterial flagella, motility, soil, structural protein
• Biological source: Achromobacter sp.
• Total number of polymer chains: 48
• Total formula weight: 2757814.70

Authors

Kreutzberger, M.A.,Wang, F.,Egelman, E.H. (deposition date: 2021-11-05, release date: 2022-03-16, Last modification date: 2024-06-05)

Primary citation

Kreutzberger, M.A.B.,Sobe, R.C.,Sauder, A.B.,Chatterjee, S.,Pena, A.,Wang, F.,Giron, J.A.,Kiessling, V.,Costa, T.R.D.,Conticello, V.P.,Frankel, G.,Kendall, M.M.,Scharf, B.E.,Egelman, E.H.
Flagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments.
Nat Commun, 13:1422-1422, 2022

PubMed Abstract: Flagellar filaments function as the propellers of the bacterial flagellum and their supercoiling is key to motility. The outer domains on the surface of the filament are non-critical for motility in many bacteria and their structures and functions are not conserved. Here, we show the atomic cryo-electron microscopy structures for flagellar filaments from enterohemorrhagic Escherichia coli O157:H7, enteropathogenic E. coli O127:H6, Achromobacter, and Sinorhizobium meliloti, where the outer domains dimerize or tetramerize to form either a sheath or a screw-like surface. These dimers are formed by 180° rotations of half of the outer domains. The outer domain sheath (ODS) plays a role in bacterial motility by stabilizing an intermediate waveform and prolonging the tumbling of E. coli cells. Bacteria with these ODS and screw-like flagellar filaments are commonly found in soil and human intestinal environments of relatively high viscosity suggesting a role for the dimerization in these environments.

PubMed: 35301306
DOI: 10.1038/s41467-022-29069-y

Experimental method

ELECTRON MICROSCOPY (3.7 Å)