title: Structure of the Neisseria meningitidis Type IV pilus.
abstract: 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 α-helix, α1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin PilE and a ∼6 Å 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 α-helices in the filament core, including a melted central portion of α1 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.
authors.affiliation: Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6.
authors.forename: Subramania
authors.initials: S
authors.lastname: Kolappan
authors.affiliation: Institut Necker-Enfants Malades, INSERM U1151, Université Paris Descartes, 14 Rue Maria Helena Vieira Da Silva, CS 61431, 75014 Paris, France.
authors.forename: Mathieu
authors.initials: M
authors.lastname: Coureuil
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.
authors.forename: Xiong
authors.initials: X
authors.lastname: Yu
authors.affiliation: Institut Necker-Enfants Malades, INSERM U1151, Université Paris Descartes, 14 Rue Maria Helena Vieira Da Silva, CS 61431, 75014 Paris, France.
authors.forename: Xavier
authors.initials: X
authors.lastname: Nassif
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.
authors.forename: Edward H
authors.initials: EH
authors.lastname: Egelman
authors.affiliation: Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6.
authors.forename: Lisa
authors.initials: L
authors.lastname: Craig
mesh_terms: D000595:Amino Acid Sequence; D020285:Cryoelectron Microscopy; D018360:Crystallography, X-Ray; D036781:Fimbriae Proteins / Q000737:chemistry*; D010861:Fimbriae, Bacterial / Q000737:chemistry*; D008958:Models, Molecular; D009344:Neisseria gonorrhoeae / Q000737:chemistry; D009345:Neisseria meningitidis / Q000737:chemistry*; D011487:Protein Conformation; D015398:Signal Transduction; D013696:Temperature
chemical_list: C429277:PilEII protein, Neisseria meningitidis; D036781:Fimbriae Proteins