EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Atomic structure of the flagellar filament reveals how ε Proteobacteria escaped Toll-like receptor 5 surveillance.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 117, Issue 29, Page 16985-16991, Year 2020
掲載日	2020年7月21日
著者	Mark A B Kreutzberger / Cheryl Ewing / Frederic Poly / Fengbin Wang / Edward H Egelman /
PubMed 要旨	Vertebrates, from zebra fish to humans, have an innate immune recognition of many bacterial flagellins. This involves a conserved eight-amino acid epitope in flagellin recognized by the Toll-like ...Vertebrates, from zebra fish to humans, have an innate immune recognition of many bacterial flagellins. This involves a conserved eight-amino acid epitope in flagellin recognized by the Toll-like receptor 5 (TLR5). Several important human pathogens, such as and , have escaped TLR5 activation by mutations in this epitope. When such mutations were introduced into flagellin, motility was abolished. It was previously argued, using very low-resolution cryoelectron microscopy (cryo-EM), that accommodated these mutations by forming filaments with 7 protofilaments, rather than the 11 found in other bacteria. We have now determined the atomic structure of the G508A flagellar filament from a 3.5-Å-resolution cryo-EM reconstruction, and show that it has 11 protofilaments. The residues in the TLR5 epitope have reduced contacts with the adjacent subunit compared to other bacterial flagellar filament structures. The weakening of the subunit-subunit interface introduced by the mutations in the TLR5 epitope is compensated for by extensive interactions between the outer domains of the flagellin subunits. In other bacteria, these outer domains can be nearly absent or removed without affecting motility. Furthermore, we provide evidence for the stabilization of these outer domain interactions through glycosylation of key residues. These results explain the essential role of glycosylation in motility, and show how the outer domains have evolved to play a role not previously found in other bacteria.
リンク	Proc Natl Acad Sci U S A / PubMed:32641510 / PubMed Central
手法	EM (らせん対称)
解像度	3.5 Å
構造データ	22088 6x80 EMDB-22088, PDB-6x80: Structure of the Campylobacter jejuni G508A Flagellar Filament 手法: EM (らせん対称) / 解像度: 3.5 Å
化合物	ChemComp-P8E: 5,7-diamino-3,5,7,9-tetradeoxy-L-glycero-alpha-L-manno-non-2-ulopyranosonic acid / 2,4α-ジヒドロキシ-5α-アミノ-6α-[(1S,2S)-1-アミノ-2-ヒドロキシプロピル]テトラヒドロ-2H-(以下略)
由来	campylobacter jejuni (カンピロバクター)
キーワード	STRUCTURAL PROTEIN / Helical Symmetry / Bacterial Flagellar Filament