9ATL

Cryo-EM of Stenotrophomonas maltophilia flagellum

9ATL の概要

• エントリーDOI: 10.2210/pdb9atl/pdb
• EMDBエントリー: 43830
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: flagellum, flagellar filament, filament, helical symmetry, protein fibril
• 由来する生物種: Stenotrophomonas maltophilia
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 441643.73

構造登録者

Fields, J.L.,Zhang, H.,Halder, S.K.,Wu, H.,Wang, F. (登録日: 2024-02-27, 公開日: 2024-11-13, 最終更新日: 2025-05-28)

主引用文献

Fields, J.L.,Zhang, H.,Bellis, N.F.,Petersen, H.A.,Halder, S.K.,Rich-New, S.T.,Krupovic, M.,Wu, H.,Wang, F.
Structural diversity and clustering of bacterial flagellar outer domains.
Nat Commun, 15:9500-9500, 2024

PubMed 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.

PubMed: 39489766
DOI: 10.1038/s41467-024-53923-w

実験手法

ELECTRON MICROSCOPY (3.26 Å)