3SOK

Dichelobacter nodosus pilin FimA

Summary for 3SOK

• Entry DOI: 10.2210/pdb3sok/pdb
• Related: 3SOJ
• Descriptor: Fimbrial protein (2 entities in total)
• Functional Keywords: pilus subunit, extracellular, cell adhesion
• Biological source: Dichelobacter nodosus
• Cellular location: Fimbrium: P02975
• Total number of polymer chains: 2
• Total formula weight: 32216.48

Authors

Arvai, A.S.,Craig, L.,Hartung, S.,Wood, T.,Kolappan, S.,Shin, D.S.,Tainer, J.A. (deposition date: 2011-06-30, release date: 2011-11-02, Last modification date: 2024-10-16)

Primary citation

Hartung, S.,Arvai, A.S.,Wood, T.,Kolappan, S.,Shin, D.S.,Craig, L.,Tainer, J.A.
Ultrahigh Resolution and Full-length Pilin Structures with Insights for Filament Assembly, Pathogenic Functions, and Vaccine Potential.
J.Biol.Chem., 286:44254-44265, 2011

PubMed Abstract: Pilin proteins assemble into Type IV pili (T4P), surface-displayed bacterial filaments with virulence functions including motility, attachment, transformation, immune escape, and colony formation. However, challenges in crystallizing full-length fiber-forming and membrane protein pilins leave unanswered questions regarding pilin structures, assembly, functions, and vaccine potential. Here we report pilin structures of full-length DnFimA from the sheep pathogen Dichelobacter nodosus and FtPilE from the human pathogen Francisella tularensis at 2.3 and 1 Å resolution, respectively. The DnFimA structure reveals an extended kinked N-terminal α-helix, an unusual centrally located disulfide, conserved subdomains, and assembled epitopes informing serogroup vaccines. An interaction between the conserved Glu-5 carboxyl oxygen and the N-terminal amine of an adjacent subunit in the crystallographic dimer is consistent with the hypothesis of a salt bridge between these groups driving T4P assembly. The FtPilE structure identifies an authentic Type IV pilin and provides a framework for understanding the role of T4P in F. tularensis virulence. Combined results define a unified pilin architecture, specialized subdomain roles in pilus assembly and function, and potential therapeutic targets.

PubMed: 22027840
DOI: 10.1074/jbc.M111.297242

Experimental method

X-RAY DIFFRACTION (2.3 Å)