Summary for 5JW8
| Entry DOI | 10.2210/pdb5jw8/pdb |
| Descriptor | Major pilin PilE (2 entities in total) |
| Functional Keywords | type iv pilin, cell adhesion |
| Biological source | Neisseria meningitidis serogroup C |
| Total number of polymer chains | 1 |
| Total formula weight | 14476.02 |
| Authors | Kolappan, S.,Craig, L. (deposition date: 2016-05-11, release date: 2016-07-06, Last modification date: 2024-11-13) |
| 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 Cited by 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: 27698424DOI: 10.1038/ncomms13015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.439 Å) |
Structure validation
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