7SN7
Cryo-EM structure of the enteropathogenic E. coli O127:H6 flagellar filament
Summary for 7SN7
| Entry DOI | 10.2210/pdb7sn7/pdb |
| EMDB information | 25213 |
| Descriptor | Flagellin (1 entity in total) |
| Functional Keywords | bacteria flagellar filament, motility, flagellar polymorphism, structural protein |
| Biological source | Escherichia coli O127:H6 |
| Total number of polymer chains | 23 |
| Total formula weight | 1291213.79 |
| Authors | Kreutzberger, M.A.B.,Chatterjee, S.,Frankel, G.,Egelman, E.H. (deposition date: 2021-10-27, 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 Cited by 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: 35301306DOI: 10.1038/s41467-022-29069-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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