6to1 | pdb_00006to1
Crystal structure of three N-terminal domains of the type V pili tip protein Mfa5 from Porphyromonas gingivalis
Structural highlights
FunctionMFA5_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).[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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