5a0l: Difference between revisions
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<StructureSection load='5a0l' size='340' side='right'caption='[[5a0l]], [[Resolution|resolution]] 1.35Å' scene=''> | <StructureSection load='5a0l' size='340' side='right'caption='[[5a0l]], [[Resolution|resolution]] 1.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a0l]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5a0l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_MGAS2096 Streptococcus pyogenes MGAS2096]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A0L FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5a0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a0l OCA], [https://pdbe.org/5a0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a0l RCSB], [https://www.ebi.ac.uk/pdbsum/5a0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a0l ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0M3KL43_STRPB A0A0M3KL43_STRPB] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus pyogenes MGAS2096]] | ||
[[Category: Banfield | [[Category: Banfield MJ]] | ||
[[Category: Dziewulska | [[Category: Dziewulska AM]] | ||
[[Category: Edwards | [[Category: Edwards JM]] | ||
[[Category: Kan | [[Category: Kan S-Y]] | ||
[[Category: Schwarz-Linek | [[Category: Schwarz-Linek U]] | ||
[[Category: Walden | [[Category: Walden M]] | ||
Revision as of 10:50, 18 May 2023
N-terminal thioester domain of fibronectin-binding protein SfbI from Streptococcus pyogenesN-terminal thioester domain of fibronectin-binding protein SfbI from Streptococcus pyogenes
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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