5ZIY

Crystal structure of Bacillus cereus FlgL

5ZIY の概要

• エントリーDOI: 10.2210/pdb5ziy/pdb
• 分子名称: Flagellar hook-associated protein 3, ZINC ION (3 entities in total)
• 機能のキーワード: flagellum, junction, structural protein
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47712.53

構造登録者

Hong, H.J.,Kim, T.H.,Song, W.S.,Yoon, S.I. (登録日: 2018-03-18, 公開日: 2018-10-17, 最終更新日: 2024-03-27)

主引用文献

Hong, H.J.,Kim, T.H.,Song, W.S.,Ko, H.J.,Lee, G.S.,Kang, S.G.,Kim, P.H.,Yoon, S.I.
Crystal structure of FlgL and its implications for flagellar assembly
Sci Rep, 8:14307-14307, 2018

PubMed Abstract: Bacteria move toward attractants and away from repellants by rotating their flagellum. The bacterial flagellum assembles through the ordered organization of more than 30 different proteins. Among the diverse flagellar proteins, FlgL forms the junction between the hook and the filament in the flagellum together with FlgK and provides a structural base where flagellin, a filament-forming protein, is inserted for the initiation of filament elongation. However, the functional and structural information available for FlgL is highly limited. To provide structural insights into the cross-linkage between the FlgL junction and the flagellin filament, we determined the crystal structures of FlgL from gram-positive Bacillus cereus (bcFlgL) and gram-negative Xanthomonas campestris (xcFlgL). bcFlgL contains one domain (D1), whereas xcFlgL adopts a two-domain structure that consists of the D1 and D2 domains. The constant D1 domain of FlgL adopts a rod structure that is generated by four longitudinal segments. This four-segment structure is recapitulated in filament and junction proteins but not in hook and rod proteins, allowing us to propose a junction-filament assembly mechanism based on a quasi-homotypic interaction. The D2 domain of xcFlgL resembles that of another junction protein, FlgK, suggesting the structural and functional relatedness of FlgL and FlgK.

PubMed: 30250171
DOI: 10.1038/s41598-018-32460-9

実験手法

X-RAY DIFFRACTION (2.2 Å)