5lo7: Difference between revisions
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<StructureSection load='5lo7' size='340' side='right'caption='[[5lo7]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='5lo7' size='340' side='right'caption='[[5lo7]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lo7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5lo7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LO7 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]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</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=5lo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo7 OCA], [https://pdbe.org/5lo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lo7 RCSB], [https://www.ebi.ac.uk/pdbsum/5lo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MYFA_YEREN MYFA_YEREN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Yersinia enterocolitica]] | ||
[[Category: | [[Category: Pakharukova NA]] | ||
[[Category: | [[Category: Roy S]] | ||
[[Category: | [[Category: Tuitilla M]] | ||
[[Category: | [[Category: Zavialov AV]] | ||
Latest revision as of 21:37, 18 October 2023
Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from Yersinia enterocoliticaCrystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from Yersinia enterocolitica
Structural highlights
FunctionPublication Abstract from PubMedThree pathogenic species of the genus Yersinia assemble adhesive fimbriae via the FGL-chaperone/usher pathway. Closely related Y. pestis and Y. pseudotuberculosis elaborate the pH6 antigen (Psa), which mediates bacterial attachment to alveolar cells of the lung. Y. enterocolitica, instead, assembles the homologous fimbriae Myf of unknown function. Here, we discovered that Myf, like Psa, specifically recognizes beta1-3- or beta1-4-linked galactose in glycosphingolipids, but completely lacks affinity for phosphatidylcholine, the main receptor for Psa in alveolar cells. The crystal structure of a subunit of Psa (PsaA) complexed with choline together with mutagenesis experiments revealed that PsaA has four phosphatidylcholine binding pockets that enable super-high-avidity binding of Psa-fibers to cell membranes. The pockets are arranged as six tyrosine residues, which are all missing in the MyfA subunit of Myf. On the other hand, the crystal structure of the MyfA-galactose complex revealed that the galactose-binding site is more extended in MyfA, enabling tighter binding to lactosyl moieties. Our results suggest that during evolution, Psa has acquired a tyrosine-rich surface that enables it to bind to phosphatidylcholine and mediate adhesion of Y. pestis/pseudotuberculosis to alveolar cells, whereas Myf has specialized as a carbohydrate-binding adhesin, facilitating the attachment of Y. enterocolitica to intestinal cells. This article is protected by copyright. All rights reserved. Structural basis for Myf and Psa fimbriae-mediated tropism of pathogenic strains of Yersinia for host tissues.,Pakharukova N, Roy S, Tuittila M, Rahman MM, Paavilainen S, Ingars AK, Skaldin M, Lamminmaki U, Hard T, Teneberg S, Zavialov AV Mol Microbiol. 2016 Aug 10. doi: 10.1111/mmi.13481. PMID:27507539[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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