5VXX
Cryo-EM reconstruction of Neisseria gonorrhoeae Type IV pilus
Summary for 5VXX
| Entry DOI | 10.2210/pdb5vxx/pdb |
| EMDB information | 8739 8740 |
| Descriptor | Fimbrial protein, alpha-D-galactopyranose-(1-3)-2,4-bisacetamido-2,4,6-trideoxy-beta-D-glucopyranose, PHOSPHORIC ACID MONO-(2-AMINO-ETHYL) ESTER (3 entities in total) |
| Functional Keywords | melted helix, type iv pili, protein fibril |
| Biological source | Neisseria gonorrhoeae |
| Total number of polymer chains | 21 |
| Total formula weight | 372664.55 |
| Authors | Wang, F.,Orlova, A.,Altindal, T.,Craig, L.,Egelman, E.H. (deposition date: 2017-05-24, release date: 2017-07-12, Last modification date: 2025-04-09) |
| Primary citation | Wang, F.,Coureuil, M.,Osinski, T.,Orlova, A.,Altindal, T.,Gesbert, G.,Nassif, X.,Egelman, E.H.,Craig, L. Cryoelectron Microscopy Reconstructions of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV Pili at Sub-nanometer Resolution. Structure, 25:1423-1435.e4, 2017 Cited by PubMed Abstract: We report here cryoelectron microscopy reconstructions of type IV pili (T4P) from two important human pathogens, Pseudomonas aeruginosa and Neisseria gonorrhoeae, at ∼ 8 and 5 Å resolution, respectively. The two structures reveal distinct arrangements of the pilin globular domains on the pilus surfaces, which impart different helical parameters, but similar packing of the conserved N-terminal α helices, α1, in the filament core. In contrast to the continuous α helix seen in the X-ray crystal structures of the P. aeruginosa and N. gonorrhoeae pilin subunits, α1 in the pilus filaments has a melted segment located between conserved helix-breaking residues Gly14 and Pro22, as seen for the Neisseria meningitidis T4P. Using mutagenesis we show that Pro22 is critical for pilus assembly, as are Thr2 and Glu5, which are positioned to interact in the hydrophobic filament core. These structures provide a framework for understanding T4P assembly, function, and biophysical properties. PubMed: 28877506DOI: 10.1016/j.str.2017.07.016 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (5.1 Å) |
Structure validation
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