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5dhm

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Crystal structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis

Structural highlights

5dhm is a 4 chain structure with sequence from Porphyromonas gingivalis ATCC 33277. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MFA4_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:19589838, PubMed:26001707). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors (Probable).^[1] ^[2]

Publication Abstract from PubMed

Gingivitis and periodontitis are chronic inflammatory diseases that can lead to tooth loss. One of the causes of these diseases is the Gram-negative Porphyromonas gingivalis. This periodontal pathogen is dependent on two fimbriae, FimA and Mfa1, for binding to dental biofilm, salivary proteins, and host cells. These fimbriae are composed of five proteins each, but the fimbriae assembly mechanism and ligands are unknown. Here we reveal the crystal structure of the precursor form of Mfa4, one of the accessory proteins of the Mfa1 fimbria. Mfa4 consists of two beta-sandwich domains and the first part of the structure forms two well-defined beta-strands that run over both domains. This N-terminal region is cleaved by gingipains, a family of proteolytic enzymes that encompass arginine- and lysine-specific proteases. Cleavage of the N-terminal region generates the mature form of the protein. Our structural data allow us to propose that the new N-terminus of the mature protein may function as a donor strand in the polymerization of P. gingivalis fimbriae.

Structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis in its precursor form: implications for a donor-strand complementation mechanism.,Kloppsteck P, Hall M, Hasegawa Y, Persson K Sci Rep. 2016 Mar 14;6:22945. doi: 10.1038/srep22945. PMID:26972441^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hasegawa Y, Iwami J, Sato K, Park Y, Nishikawa K, Atsumi T, Moriguchi K, Murakami Y, Lamont RJ, Nakamura H, Ohno N, Yoshimura F. Anchoring and length regulation of Porphyromonas gingivalis Mfa1 fimbriae by the downstream gene product Mfa2. Microbiology. 2009 Oct;155(Pt 10):3333-47. doi: 10.1099/mic.0.028928-0. Epub 2009, Jul 9. PMID:19589838 doi:http://dx.doi.org/10.1099/mic.0.028928-0
↑ 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
↑ Kloppsteck P, Hall M, Hasegawa Y, Persson K. Structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis in its precursor form: implications for a donor-strand complementation mechanism. Sci Rep. 2016 Mar 14;6:22945. doi: 10.1038/srep22945. PMID:26972441 doi:http://dx.doi.org/10.1038/srep22945

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5dhm"

Categories: Large Structures | Porphyromonas gingivalis ATCC 33277 | Hall M | Kloppsteck P | Persson K

@@ Line 1: / Line 1: @@
 ==Crystal structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis==
-<StructureSection load='5dhm' size='340' side='right' caption='[[5dhm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='5dhm' size='340' side='right'caption='[[5dhm]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5dhm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DHM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DHM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5dhm]] is a 4 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=5DHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DHM FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.9&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhm OCA], [http://pdbe.org/5dhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dhm RCSB], [http://www.ebi.ac.uk/pdbsum/5dhm PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5dhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dhm OCA], [https://pdbe.org/5dhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dhm RCSB], [https://www.ebi.ac.uk/pdbsum/5dhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dhm ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/MFA4_PORG3 MFA4_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:19589838, PubMed:26001707). They play an important role in invasion of periodontal tissues and are recognized as major virulence factors (Probable).<ref>PMID:19589838</ref> <ref>PMID:26001707</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Hall, M]]
+[[Category: Large Structures]]
-[[Category: Kloppsteck, P]]
+[[Category: Porphyromonas gingivalis ATCC 33277]]
-[[Category: Persson, K]]
+[[Category: Hall M]]
-[[Category: Adhesin]]
+[[Category: Kloppsteck P]]
-[[Category: Cell adhesion]]
+[[Category: Persson K]]
-[[Category: Fimbria]]
-[[Category: Periodontitis]]

5dhm

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Current revision

Crystal structure of the fimbrial protein Mfa4 from Porphyromonas gingivalis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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