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| | <StructureSection load='5nf4' size='340' side='right'caption='[[5nf4]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='5nf4' size='340' side='right'caption='[[5nf4]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nf4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NF4 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NF4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porphyromonas_gingivalis_ATCC_33277 Porphyromonas gingivalis ATCC 33277]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NF4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.746Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5nf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf4 OCA], [http://pdbe.org/5nf4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nf4 RCSB], [http://www.ebi.ac.uk/pdbsum/5nf4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf4 ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5nf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nf4 OCA], [https://pdbe.org/5nf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nf4 RCSB], [https://www.ebi.ac.uk/pdbsum/5nf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nf4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MFA3_PORG3 MFA3_PORG3]] Tip 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:24118823, 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:24118823</ref> <ref>PMID:26001707</ref> | + | [https://www.uniprot.org/uniprot/MFA3_PORG3 MFA3_PORG3] Tip 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:24118823, 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:24118823</ref> <ref>PMID:26001707</ref> |
| | <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: Hall, M]] | + | [[Category: Porphyromonas gingivalis ATCC 33277]] |
| - | [[Category: Hasegawa, Y]] | + | [[Category: Hall M]] |
| - | [[Category: Persson, K]] | + | [[Category: Hasegawa Y]] |
| - | [[Category: Yoshimura, F]] | + | [[Category: Persson K]] |
| - | [[Category: Adhesin]]
| + | [[Category: Yoshimura F]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Fimbria]]
| + | |
| - | [[Category: Periodontitis]]
| + | |
| Structural highlights
Function
MFA3_PORG3 Tip 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:24118823, 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).[1] [2]
Publication Abstract from PubMed
Very little is known about how fimbriae of Bacteroidetes bacteria are assembled. To shed more light on this process, we solved the crystal structures of the shaft protein Mfa1, the regulatory protein Mfa2, and the tip protein Mfa3 from the periodontal pathogen Porphyromonas gingivalis. Together these build up part of the Mfa1 fimbria and represent three of the five proteins, Mfa1-5, encoded by the mfa1 gene cluster. Mfa1, Mfa2 and Mfa3 have the same overall fold i.e., two beta-sandwich domains. Upon polymerization, the first beta-strand of the shaft or tip protein is removed by indigenous proteases. Although the resulting void is expected to be filled by a donor-strand from another fimbrial protein, the mechanism by which it does so is still not established. In contrast, the first beta-strand in Mfa2, the anchoring protein, is firmly attached by a disulphide bond and is not cleaved. Based on the structural information, we created multiple mutations in P. gingivalis and analysed their effect on fimbrial polymerization and assembly in vivo. Collectively, these data suggest an important role for the C-terminal tail of Mfa1, but not of Mfa3, affecting both polymerization and maturation of downstream fimbrial proteins.
Structural and functional characterization of shaft, anchor, and tip proteins of the Mfa1 fimbria from the periodontal pathogen Porphyromonas gingivalis.,Hall M, Hasegawa Y, Yoshimura F, Persson K Sci Rep. 2018 Jan 29;8(1):1793. doi: 10.1038/s41598-018-20067-z. PMID:29379120[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hasegawa Y, Nagano K, Ikai R, Izumigawa M, Yoshida Y, Kitai N, Lamont RJ, Murakami Y, Yoshimura F. Localization and function of the accessory protein Mfa3 in Porphyromonas gingivalis Mfa1 fimbriae. Mol Oral Microbiol. 2013 Dec;28(6):467-80. doi: 10.1111/omi.12040. Epub 2013 Oct , 5. PMID:24118823 doi:http://dx.doi.org/10.1111/omi.12040
- ↑ Nagano K, Hasegawa Y, Yoshida Y, Yoshimura F. A Major Fimbrilin Variant of Mfa1 Fimbriae in Porphyromonas gingivalis. J Dent Res. 2015 Aug;94(8):1143-8. doi: 10.1177/0022034515588275. Epub 2015 May, 22. PMID:26001707 doi:http://dx.doi.org/10.1177/0022034515588275
- ↑ Hall M, Hasegawa Y, Yoshimura F, Persson K. Structural and functional characterization of shaft, anchor, and tip proteins of the Mfa1 fimbria from the periodontal pathogen Porphyromonas gingivalis. Sci Rep. 2018 Jan 29;8(1):1793. doi: 10.1038/s41598-018-20067-z. PMID:29379120 doi:http://dx.doi.org/10.1038/s41598-018-20067-z
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