Structural diversity and clustering of bacterial flagellar outer domains

Jessie Lynda Fields, Hua Zhang, Nathan F. Bellis, Holly A. Petersen, Sajal K. Halder, Shane T. Rich-New, Mart Krupovic, Hui Wu () and Fengbin Wang ()
Additional contact information
Jessie Lynda Fields: University of Alabama at Birmingham
Hua Zhang: Oregon Health & Science University
Nathan F. Bellis: University of Alabama at Birmingham
Holly A. Petersen: University of Alabama at Birmingham
Sajal K. Halder: University of Alabama at Birmingham
Shane T. Rich-New: University of Alabama at Birmingham
Mart Krupovic: Archaeal Virology Unit
Hui Wu: Oregon Health & Science University
Fengbin Wang: University of Alabama at Birmingham

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract 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.

Date: 2024
References: View references in EconPapers View complete reference list from CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-024-53923-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53923-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-024-53923-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().