Structural diversity and clustering of bacterial flagellar outer domains

Fields, Jessie Lynda; Zhang, Hua; Bellis, Nathan F.; Petersen, Holly A.; Halder, Sajal K.; Rich-New, Shane T.; Krupovic, Mart; Wu, Hui; Wang, Fengbin

doi:10.1038/s41467-024-53923-w

Structural diversity and clustering of bacterial flagellar outer domains

Journal Article · Sun Nov 03 00:00:00 EDT 2024 · Nature Communications

DOI:https://doi.org/10.1038/s41467-024-53923-w· OSTI ID:3005566

Fields, Jessie Lynda ^[1]; Zhang, Hua ^[2]; Bellis, Nathan F. ^[1]; Petersen, Holly A. ^[1]; ^[1]; ^[1]; ^[3]; ^[2]; ^[1]

Univ. of Alabama, Birmingham, AL (United States)
Oregon Health & Science Univ., Portland, OR (United States)
Paris Cité Univ. (France)

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.

View Accepted Manuscript (DOE)

Research Organization:: Univ. of California, Irvine, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES). Chemical Sciences, Geosciences & Biosciences Division (CSGB)

Grant/Contract Number:: SC0020322; SC0024303

OSTI ID:: 3005566

Journal Information:: Nature Communications, Journal Name: Nature Communications Journal Issue: 1 Vol. 15; ISSN 2041-1723

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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