5A0G

N-terminal thioester domain of surface protein from Clostridium perfringens

5A0G の概要

• エントリーDOI: 10.2210/pdb5a0g/pdb
• 関連するPDBエントリー: 5A0D 5A0L 5A0N
• 分子名称: SURFACE ANCHORED PROTEIN (2 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: CLOSTRIDIUM PERFRINGENS
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 127709.90

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: 2015-04-20, 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

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

実験手法

X-RAY DIFFRACTION (2.62 Å)