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==N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae== | ==N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae== | ||
<StructureSection load='5a0n' size='340' side='right' caption='[[5a0n]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='5a0n' size='340' side='right'caption='[[5a0n]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a0n]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0N OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5a0n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_SP14-BS69 Streptococcus pneumoniae SP14-BS69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0N FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0n OCA], [https://pdbe.org/5a0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0n RCSB], [https://www.ebi.ac.uk/pdbsum/5a0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A5MCJ6_STREE A5MCJ6_STREE] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:26032562</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5a0n" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Streptococcus pneumoniae SP14-BS69]] | |||
[[Category: | [[Category: Banfield MJ]] | ||
[[Category: Dziewulska AM]] | |||
[[Category: Edwards JM]] | |||
[[Category: | [[Category: Kan S-Y]] | ||
[[Category: | [[Category: Schwarz-Linek U]] | ||
[[Category: | [[Category: Walden M]] | ||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 14:34, 9 May 2024
N-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniaeN-terminal thioester domain of protein F2 like fibronectin-binding protein from Streptococcus pneumoniae
Structural highlights
FunctionPublication Abstract from PubMedTo 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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