5GY2

Crystal structure of a complex between Bacillus subtilis flagellin and zebrafish Toll-like receptor 5

5GY2 の概要

• エントリーDOI: 10.2210/pdb5gy2/pdb
• 分子名称: Tlr5b protein,Variable lymphocyte receptor B, Flagellin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: bacterial protein immune receptor, immune system
• 由来する生物種: Danio rerio (Zebrafish); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143411.26

構造登録者

Song, W.S.,Yoon, S.I. (登録日: 2016-09-21, 公開日: 2017-02-15, 最終更新日: 2024-11-06)

主引用文献

Song, W.S.,Jeon, Y.J.,Namgung, B.,Hong, M.,Yoon, S.I.
A conserved TLR5 binding and activation hot spot on flagellin
Sci Rep, 7:40878-40878, 2017

PubMed Abstract: Flagellin is a bacterial protein that polymerizes into the flagellar filament and is essential for bacterial motility. When flagellated bacteria invade the host, flagellin is recognized by Toll-like receptor 5 (TLR5) as a pathogen invasion signal and eventually evokes the innate immune response. Here, we provide a conserved structural mechanism by which flagellins from Gram-negative γ-proteobacteria and Gram-positive Firmicutes bacteria bind and activate TLR5. The comparative structural analysis using our crystal structure of a complex between Bacillus subtilis flagellin (bsflagellin) and TLR5 at 2.1 Å resolution, combined with the alanine scanning analysis of the binding interface, reveals a common hot spot in flagellin for TLR5 activation. An arginine residue (bsflagellin R89) of the flagellin D1 domain and its adjacent residues (bsflagellin E114 and L93) constitute a hot spot that provides shape and chemical complementarity to a cavity generated by the loop of leucine-rich repeat 9 in TLR5. In addition to the flagellin D1 domain, the D0 domain also contributes to TLR5 activity through structurally dispersed regions, but not a single focal area. These results establish the groundwork for the future design of flagellin-based therapeutics.

PubMed: 28106112
DOI: 10.1038/srep40878

実験手法

X-RAY DIFFRACTION (2.1 Å)