Structural highlights
Function[FMM1_NEIGO] This protein is the predominant Neisseria surface antigen, which allows adhesion of the bacterium to various host cells. Publication Abstract from PubMedWe report here cryoelectron microscopy reconstructions of type IV pili (T4P) from two important human pathogens, Pseudomonas aeruginosa and Neisseria gonorrhoeae, at approximately 8 and 5 A resolution, respectively. The two structures reveal distinct arrangements of the pilin globular domains on the pilus surfaces, which impart different helical parameters, but similar packing of the conserved N-terminal alpha helices, alpha1, in the filament core. In contrast to the continuous alpha helix seen in the X-ray crystal structures of the P. aeruginosa and N. gonorrhoeae pilin subunits, alpha1 in the pilus filaments has a melted segment located between conserved helix-breaking residues Gly14 and Pro22, as seen for the Neisseria meningitidis T4P. Using mutagenesis we show that Pro22 is critical for pilus assembly, as are Thr2 and Glu5, which are positioned to interact in the hydrophobic filament core. These structures provide a framework for understanding T4P assembly, function, and biophysical properties. Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution.,Wang F, Coureuil M, Osinski T, Orlova A, Altindal T, Gesbert G, Nassif X, Egelman EH, Craig L Structure. 2017 Sep 5;25(9):1423-1435.e4. doi: 10.1016/j.str.2017.07.016. PMID:28877506[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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