7C7Z

Crystal structure of the flagellar junction protein FlgL from Legionella pneumophila

7C7Z の概要

• エントリーDOI: 10.2210/pdb7c7z/pdb
• 分子名称: Flagellar hook-associated protein 3 (2 entities in total)
• 機能のキーワード: flgl, legionella pneumophila, structural protein
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72418.27

構造登録者

Song, W.S.,Hong, H.J.,Yoon, S.I. (登録日: 2020-05-27, 公開日: 2020-08-12, 最終更新日: 2023-11-29)

主引用文献

Song, W.S.,Hong, H.J.,Yoon, S.I.
Structural study of the flagellar junction protein FlgL from Legionella pneumophila.
Biochem.Biophys.Res.Commun., 529:513-518, 2020

PubMed Abstract: Legionella pneumophila is a flagellated pathogenic bacterium that causes atypical pneumonia called Legionnaires' disease. The flagellum plays a key role in the pathogenesis of L. pneumophila in the host. The protein FlgL forms a junction between the flagellar hook and filament and has been reported to elicit the host humoral immune response. To provide structural insights into FlgL-mediated junction assembly and FlgL-based vaccine design, we performed structural and serological studies on L. pneumophila FlgL (lpFlgL). The crystal structure of a truncated lpFlgL protein that consists of the D1 and D2 domains was determined at 3.06 Å resolution. The D1 domain of lpFlgL adopts a primarily helical, rod-shaped structure, and the D2 domain folds into a β-sandwich structure that is affixed to the upper region of the D1 domain. The D1 domain of lpFlgL exhibits structural similarity to the flagellar filament protein flagellin, allowing us to propose a structural model of the lpFlgL junction based on the polymeric structure of flagellin. Furthermore, the D1 domain of lpFlgL exhibited substantially higher protein stability than the D2 domain and was responsible for most of the antigenicity of lpFlgL, suggesting that the D1 domain of lpFlgL would be a suitable target for the development of an anti-L. pneumophila vaccine.

PubMed: 32703460
DOI: 10.1016/j.bbrc.2020.06.012

実験手法

X-RAY DIFFRACTION (3.06 Å)