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Structure paper

TitleFlagellin outer domain dimerization modulates motility in pathogenic and soil bacteria from viscous environments.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1422, Year 2022
Publish dateMar 17, 2022
AuthorsMark A B Kreutzberger / Richard C Sobe / Amber B Sauder / Sharanya Chatterjee / Alejandro Peña / Fengbin Wang / Jorge A Giron / Volker Kiessling / Tiago R D Costa / Vincent P Conticello / Gad Frankel / Melissa M Kendall / Birgit E Scharf / Edward H Egelman /
PubMed AbstractFlagellar 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 ...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.
External linksNat Commun / PubMed:35301306 / PubMed Central
MethodsEM (helical sym.) / EM (single particle)
Resolution3.5 - 7.7 Å
Structure data

25211

7sn4

EMDB-25211, PDB-7sn4:
Cryo-EM structure of the enterohemorrhagic E. coli O157:H7 flagellar filament
Method: EM (helical sym.) / Resolution: 3.6 Å

EMDB-25212:
Cryo-EM structure of the N319F, N323F EHEC O157:H7 flagellar filament
Method: EM (helical sym.) / Resolution: 7.7 Å

25213

7sn7

EMDB-25213, PDB-7sn7:
Cryo-EM structure of the enteropathogenic E. coli O127:H6 flagellar filament
Method: EM (single particle) / Resolution: 4.2 Å

25215

7sn9

EMDB-25215, PDB-7sn9:
Cryo-EM structure of the Sinorhizobium meliloti flagellar filament
Method: EM (helical sym.) / Resolution: 3.5 Å

25382

7sqd

EMDB-25382, PDB-7sqd:
Cryo-EM structure of the Achromobacter flagellar filament
Method: EM (helical sym.) / Resolution: 3.7 Å

25386

7sqj

EMDB-25386, PDB-7sqj:
Cryo-EM structure of the seam subunits of the enteropathogenic E. coli O127:H6 flagellar filament
Method: EM (single particle) / Resolution: 6.3 Å

EMDB-25388:
Cryo-EM map of the EHEC O157:H7 flagellar filament outer domain sheath with D1 symmetry
Method: EM (helical sym.) / Resolution: 3.6 Å

Source
  • Escherichia coli (E. coli)
  • escherichia coli o157:h7 (bacteria)
  • escherichia coli o127:h6 (bacteria)
  • sinorhizobium meliloti (bacteria)
  • achromobacter sp. (bacteria)
KeywordsSTRUCTURAL PROTEIN / Bacteria flagellar filament / motility / flagellar polymorphism / Bacterial flagella / soil

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