6kmf
From Proteopedia
FimA type V pilus from P.gingivalis
Structural highlights
Function[FIMA1_PORG3] Structural subunit of the major fimbriae. These long, 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:9786913, PubMed:12593606, PubMed:15165251, PubMed:17675496, PubMed:17526848, PubMed:20530728, PubMed:27062925). They play an important role in the invasion of periodontal tissues (PubMed:12593606). Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification (PubMed:23809984). The sequence-based classification correlates with pathogenicity (PubMed:17675496).[1] [2] [3] [4] [5] [6] [7] [8] Publication Abstract from PubMedBacterial adhesion is a general strategy for host-microbe and microbe-microbe interactions. Adhesive pili are essential for colonization, biofilm formation, virulence and pathogenesis of many environmental and pathogenic bacteria(1,2). Members of the class Bacteroidia have unique type V pili, assembled by protease-mediated polymerization(3). Porphyromonas gingivalis is the main contributor to periodontal disease and its type V pili are a key factor for its virulence(4). However, the structure of the polymerized pilus and its assembly mechanism are unknown. Here we show structures of polymerized and monomeric states of FimA stalk pilin from P. gingivalis, determined by cryo-electron microscopy and crystallography. The atomic model of assembled FimA shows that the C-terminal strand of a donor subunit is inserted into a groove in the beta-sheet of an acceptor subunit after N-terminal cleavage by the protease RgpB. The C terminus of the donor strand is essential for polymerization. We propose that type V pili assemble via a sequential polar assembly mechanism at the cell surface, involving protease-mediated strand exchange, employed by various Gram-negative species belonging to the class Bacteroidia. Our results reveal functional surfaces related to pathogenic properties of polymerized FimA. These insights may facilitate development of antibacterial drugs. Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange.,Shibata S, Shoji M, Okada K, Matsunami H, Matthews MM, Imada K, Nakayama K, Wolf M Nat Microbiol. 2020 Apr 13. pii: 10.1038/s41564-020-0705-1. doi:, 10.1038/s41564-020-0705-1. PMID:32284566[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Porg3 | Imada, K | Matsunami, H | Matthews, M | Nakayama, K | Shibata, S | Shoji, M | Wolf, M | Atcc33277 | Cell adhesion | Fima | Porphyromonas gingivali | Type v pilus
