Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3SOJ

Francisella tularensis pilin PilE

Summary for 3SOJ
Entry DOI10.2210/pdb3soj/pdb
Related3SOK
DescriptorPilE, SULFATE ION (3 entities in total)
Functional Keywordspilus subunit, extracellular, cell adhesion
Biological sourceFrancisella tularensis subsp. tularensis
Total number of polymer chains2
Total formula weight24454.59
Authors
Wood, T.,Arvai, A.S.,Shin, D.S.,Hartung, S.,Kolappan, S.,Craig, L.,Tainer, J.A. (deposition date: 2011-06-30, release date: 2011-11-02, Last modification date: 2024-10-30)
Primary citationHartung, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1 Å)
Structure validation

227344

건을2024-11-13부터공개중

PDB statisticsPDBj update infoContact PDBjnumon