5KUA

Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus

Summary for 5KUA

• Entry DOI: 10.2210/pdb5kua/pdb
• EMDB information: 8287
• Descriptor: pilin (1 entity in total)
• Functional Keywords: melted helix, type iv pili, protein fibril
• Biological source: Neisseria meningitidis
• Total number of polymer chains: 26
• Total formula weight: 443746.73

Authors

Kolappan, S.,Coureuil, M.,Yu, X.,Nassif, X.,Craig, L.,Egelman, E.H. (deposition date: 2016-07-13, release date: 2016-10-12, Last modification date: 2024-10-16)

Primary citation

Kolappan, S.,Coureuil, M.,Yu, X.,Nassif, X.,Egelman, E.H.,Craig, L.
Structure of the Neisseria meningitidis Type IV pilus.
Nat Commun, 7:13015-13015, 2016

PubMed 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.

PubMed: 27698424
DOI: 10.1038/ncomms13015

Experimental method

ELECTRON MICROSCOPY (6 Å)