5A0N

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

Summary for 5A0N

• Entry DOI: 10.2210/pdb5a0n/pdb
• Related: 5A0D 5A0G 5A0L
• Descriptor: PROTEIN F2 LIKE FIBRONECTIN-BINDING PROTEIN, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, GLYCEROL, ... (4 entities in total)
• Functional Keywords: cell adhesion, surface-associated protein, gram-positive, adhesin, internal thioester, thioester domain
• Biological source: STREPTOCOCCUS PNEUMONIAE
• Total number of polymer chains: 1
• Total formula weight: 26096.33

Authors

Walden, M.,Edwards, J.M.,Dziewulska, A.M.,Kan, S.-Y.,Schwarz-Linek, U.,Banfield, M.J. (deposition date: 2015-04-21, release date: 2015-06-03, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.3 Å)