6tnj
From Proteopedia
(Difference between revisions)
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==Crystal structure of the vWF domain of the type V pili tip protein Mfa5 from Porphyromonas gingivalis== | ==Crystal structure of the vWF domain of the type V pili tip protein Mfa5 from Porphyromonas gingivalis== | ||
- | <StructureSection load='6tnj' size='340' side='right'caption='[[6tnj]]' scene=''> | + | <StructureSection load='6tnj' size='340' side='right'caption='[[6tnj]], [[Resolution|resolution]] 1.85Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TNJ OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6tnj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Porg3 Porg3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TNJ FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MPO:3[N-MORPHOLINO]PROPANE+SULFONIC+ACID'>MPO</scene></td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PGN_0291 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=431947 PORG3])</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=6tnj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tnj OCA], [https://pdbe.org/6tnj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tnj RCSB], [https://www.ebi.ac.uk/pdbsum/6tnj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tnj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[https://www.uniprot.org/uniprot/MFA5_PORG3 MFA5_PORG3]] Accessory subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome (PubMed:26001707). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Fimbrium subunits from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).<ref>PMID:26001707</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The Gram-negative bacterium Porphyromonas gingivalis is a secondary colonizer of the oral biofilm and is involved in the onset and progression of periodontitis. Its fimbriae, of type-V, are important for attachment to other microorganisms in the biofilm and for adhesion to host cells. The fimbriae are assembled from five proteins encoded by the mfa1 operon, of which Mfa5 is one of the ancillary tip proteins. Here we report the X-ray structure of the N-terminal half of Mfa5, which reveals a von Willebrand factor domain and two IgG-like domains. One of the IgG-like domains is stabilized by an intramolecular isopeptide bond, which is the first such bond observed in a Gram-negative bacterium. These features make Mfa5 structurally more related to streptococcal adhesins than to the other P. gingivalis Mfa proteins. The structure reported here indicates that horizontal gene transfer has occurred among the bacteria within the oral biofilm. | ||
+ | |||
+ | Porphyromonas gingivalis fimbrial protein Mfa5 contains a von Willebrand factor domain and an intramolecular isopeptide.,Heidler TV, Ernits K, Ziolkowska A, Claesson R, Persson K Commun Biol. 2021 Jan 25;4(1):106. doi: 10.1038/s42003-020-01621-w. PMID:33495563<ref>PMID:33495563</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6tnj" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Claesson R]] | + | [[Category: Porg3]] |
- | [[Category: Heidler | + | [[Category: Claesson, R]] |
- | [[Category: Persson K]] | + | [[Category: Heidler, T V]] |
+ | [[Category: Persson, K]] | ||
+ | [[Category: Bacterial adhesion]] | ||
+ | [[Category: Cell adhesion]] | ||
+ | [[Category: Intramolekular isopeptide]] | ||
+ | [[Category: Mfa1 fimbriae]] | ||
+ | [[Category: Phorphyromonas gingivali]] | ||
+ | [[Category: Type v pili]] | ||
+ | [[Category: Von willebrand factor]] |
Current revision
Crystal structure of the vWF domain of the type V pili tip protein Mfa5 from Porphyromonas gingivalis
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