7SN7

Cryo-EM structure of the enteropathogenic E. coli O127:H6 flagellar filament

7SN7 の概要

• エントリーDOI: 10.2210/pdb7sn7/pdb
• EMDBエントリー: 25213
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: bacteria flagellar filament, motility, flagellar polymorphism, structural protein
• 由来する生物種: Escherichia coli O127:H6
• タンパク質・核酸の鎖数: 23
• 化学式量合計: 1291213.79

構造登録者

Kreutzberger, M.A.B.,Chatterjee, S.,Frankel, G.,Egelman, E.H. (登録日: 2021-10-27, 公開日: 2022-03-16, 最終更新日: 2024-06-05)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (4.2 Å)