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5A0N

N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae

5A0N の概要
エントリーDOI10.2210/pdb5a0n/pdb
関連するPDBエントリー5A0D 5A0G 5A0L
分子名称PROTEIN F2 LIKE FIBRONECTIN-BINDING PROTEIN, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLYCEROL, ... (4 entities in total)
機能のキーワードcell adhesion, surface-associated protein, gram-positive, adhesin, internal thioester, thioester domain
由来する生物種STREPTOCOCCUS PNEUMONIAE
タンパク質・核酸の鎖数1
化学式量合計26096.33
構造登録者
Walden, M.,Edwards, J.M.,Dziewulska, A.M.,Kan, S.-Y.,Schwarz-Linek, U.,Banfield, M.J. (登録日: 2015-04-21, 公開日: 2015-06-03, 最終更新日: 2024-05-08)
主引用文献Walden, M.,Edwards, J.M.,Dziewulska, A.M.,Bergmann, R.,Saalbach, G.,Kan, S.Y.,Miller, O.K.,Weckener, M.,Jackson, R.J.,Shirran, S.L.,Botting, C.H.,Florence, G.J.,Rohde, M.,Banfield, M.J.,Schwarz-Linek, U.
An internal thioester in a pathogen surface protein mediates covalent host binding.
Elife, 4:-, 2015
Cited by
PubMed Abstract: To cause disease and persist in a host, pathogenic and commensal microbes must adhere to tissues. Colonization and infection depend on specific molecular interactions at the host-microbe interface that involve microbial surface proteins, or adhesins. To date, adhesins are only known to bind to host receptors non-covalently. Here we show that the streptococcal surface protein SfbI mediates covalent interaction with the host protein fibrinogen using an unusual internal thioester bond as a 'chemical harpoon'. This cross-linking reaction allows bacterial attachment to fibrin and SfbI binding to human cells in a model of inflammation. Thioester-containing domains are unexpectedly prevalent in Gram-positive bacteria, including many clinically relevant pathogens. Our findings support bacterial-encoded covalent binding as a new molecular principle in host-microbe interactions. This represents an as yet unexploited target to treat bacterial infection and may also offer novel opportunities for engineering beneficial interactions.
PubMed: 26032562
DOI: 10.7554/eLife.06638
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.3 Å)
構造検証レポート
Validation report summary of 5a0n
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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