6JZK

Structure of FimA type-1 (FimA1) prepilin of the type V major fimbrium

Summary for 6JZK

• Entry DOI: 10.2210/pdb6jzk/pdb
• Related: 6JZJ
• Descriptor: Major fimbrium subunit FimA type-1, GLYCEROL, SULFATE ION, ... (5 entities in total)
• Functional Keywords: type v pili, major fimbrial subunit protein, cell adhesion
• Biological source: Porphyromonas gingivalis ATCC 33277
• Total number of polymer chains: 2
• Total formula weight: 79612.62

Authors

Okada, K.,Shoji, M.,Nakayam, K.,Imada, K. (deposition date: 2019-05-02, release date: 2020-04-15, Last modification date: 2023-11-22)

Primary citation

Shibata, S.,Shoji, M.,Okada, K.,Matsunami, H.,Matthews, M.M.,Imada, K.,Nakayama, K.,Wolf, M.
Structure of polymerized type V pilin reveals assembly mechanism involving protease-mediated strand exchange.
Nat Microbiol, 5:830-837, 2020

PubMed Abstract: Bacterial 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. Members of the class Bacteroidia have unique type V pili, assembled by protease-mediated polymerization. Porphyromonas gingivalis is the main contributor to periodontal disease and its type V pili are a key factor for its virulence. 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 β-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.

PubMed: 32284566
DOI: 10.1038/s41564-020-0705-1

Experimental method

X-RAY DIFFRACTION (2.1 Å)