5a0d: Difference between revisions
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==N-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutant== | ==N-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutant== | ||
<StructureSection load='5a0d' size='340' side='right' caption='[[5a0d]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='5a0d' size='340' side='right'caption='[[5a0d]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a0d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0D OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5a0d]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_B Clostridium perfringens B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0D 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]] 1.6Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5a0d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0d OCA], [https://pdbe.org/5a0d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0d RCSB], [https://www.ebi.ac.uk/pdbsum/5a0d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B1R775_CLOPF B1R775_CLOPF] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 5a0d" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Clostridium perfringens B]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Banfield MJ]] | ||
[[Category: | [[Category: Dziewulska AM]] | ||
[[Category: | [[Category: Edwards JM]] | ||
[[Category: | [[Category: Kan S-Y]] | ||
[[Category: Schwarz-Linek U]] | |||
[[Category: Walden M]] | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 14:34, 9 May 2024
N-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutantN-terminal thioester domain of surface protein from Clostridium perfringens, Cys138Ala mutant
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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