Structure of the Neisseria meningitidis Type IV pilus - Archive ouverte HAL
Article Dans Une Revue Nature Communications Année : 2016

Structure of the Neisseria meningitidis Type IV pilus

Résumé

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 a-helix, a1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin PilE and a B6 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 a-helices in the filament core, including a melted central portion of a1 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.
Fichier principal
Vignette du fichier
ncomms13015.pdf (2.6 Mo) Télécharger le fichier
Origine Fichiers éditeurs autorisés sur une archive ouverte

Dates et versions

hal-03552938 , version 1 (02-02-2022)

Identifiants

Citer

Subramania Kolappan, Mathieu Coureuil, Xiong Yu, Xavier Nassif, Edward H Egelman, et al.. Structure of the Neisseria meningitidis Type IV pilus. Nature Communications, 2016, 7, ⟨10.1038/ncomms13015⟩. ⟨hal-03552938⟩
20 Consultations
55 Téléchargements

Altmetric

Partager

More