5a0d

N-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutant

spinqualitylabelsall models 5a0d, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a0d is a 4 chain structure with sequence from Clostridium perfringens b. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO Related: 5a0g, 5a0l, 5a0n Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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. An internal thioester in a pathogen surface protein mediates covalent host binding.,Walden M, Edwards JM, Dziewulska AM, Bergmann R, Saalbach G, Kan SY, Miller OK, Weckener M, Jackson RJ, Shirran SL, Botting CH, Florence GJ, Rohde M, Banfield MJ, Schwarz-Linek U Elife. 2015 Jun 2;4. doi: 10.7554/eLife.06638. PMID:26032562 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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