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TitleStructural diversity and clustering of bacterial flagellar outer domains.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 9500, Year 2024
Publish dateNov 3, 2024
AuthorsJessie Lynda Fields / Hua Zhang / Nathan F Bellis / Holly A Petersen / Sajal K Halder / Shane T Rich-New / Mart Krupovic / Hui Wu / Fengbin Wang /
PubMed AbstractSupercoiled flagellar filaments function as mechanical propellers within the bacterial flagellum complex, playing a crucial role in motility. Flagellin, the building block of the filament, features a ...Supercoiled flagellar filaments function as mechanical propellers within the bacterial flagellum complex, playing a crucial role in motility. Flagellin, the building block of the filament, features a conserved inner D0/D1 core domain across different bacterial species. In contrast, approximately half of the flagellins possess additional, highly divergent outer domain(s), suggesting varied functional potential. In this study, we report atomic structures of flagellar filaments from three distinct bacterial species: Cupriavidus gilardii, Stenotrophomonas maltophilia, and Geovibrio thiophilus. Our findings reveal that the flagella from the facultative anaerobic G. thiophilus possesses a significantly more negatively charged surface, potentially enabling adhesion to positively charged minerals. Furthermore, we analyze all AlphaFold predicted structures for annotated bacterial flagellins, categorizing the flagellin outer domains into 682 structural clusters. This classification provides insights into the prevalence and experimental verification of these outer domains. Remarkably, two of the flagellar structures reported herein belong to a distinct cluster, indicating additional opportunities on the study of the functional diversity of flagellar outer domains. Our findings underscore the complexity of bacterial flagellins and open up possibilities for future studies into their varied roles beyond motility.
External linksNat Commun / PubMed:39489766 / PubMed Central
MethodsEM (helical sym.)
Resolution3.26 - 4.1 Å
Structure data

43829

9atb

EMDB-43829, PDB-9atb:
cryo-EM of Cupriavidus gilardii flagellum
Method: EM (helical sym.) / Resolution: 3.4 Å

43830

9atl

EMDB-43830, PDB-9atl:
Cryo-EM of Stenotrophomonas maltophilia flagellum
Method: EM (helical sym.) / Resolution: 3.26 Å

43868

9au6

EMDB-43868, PDB-9au6:
Cryo-EM of Geovibrio thiophilus flagellum
Method: EM (helical sym.) / Resolution: 4.1 Å

Source
  • cupriavidus gilardii (bacteria)
  • stenotrophomonas maltophilia (bacteria)
  • geovibrio thiophilus (bacteria)
KeywordsPROTEIN FIBRIL / Flagellum / Flagellar filament / filament / helical symmetry

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