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Publication Abstract from PubMed

Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended alpha-helix, alpha1, in X-ray crystal structures. Here we report a 1.44 A crystal structure of the N. meningitidis major pilin PilE and a approximately 6 A cryo-electron microscopy reconstruction of the intact pilus, from which we built an atomic model for the filament. This structure reveals the molecular arrangement of the N-terminal alpha-helices in the filament core, including a melted central portion of alpha1 and a bridge of electron density consistent with a predicted salt bridge necessary for pilus assembly. This structure has important implications for understanding pilus biology.

Structure of the Neisseria meningitidis Type IV pilus.,Kolappan S, Coureuil M, Yu X, Nassif X, Egelman EH, Craig L Nat Commun. 2016 Oct 4;7:13015. doi: 10.1038/ncomms13015. PMID:27698424^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.