5VXY

Cryo-EM reconstruction of PAK pilus from Pseudomonas aeruginosa

5VXY の概要

• エントリーDOI: 10.2210/pdb5vxy/pdb
• EMDBエントリー: 8739 8740
• 分子名称: Fimbrial protein (1 entity in total)
• 機能のキーワード: melted helix, type iv pili, protein fibril
• 由来する生物種: Pseudomonas aeruginosa PAK
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 315444.78

構造登録者

Wang, F.,Osinksi, T.,Orlova, A.,Altindal, T.,Craig, L.,Egelman, E.H. (登録日: 2017-05-24, 公開日: 2017-07-12, 最終更新日: 2024-11-20)

主引用文献

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

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: 28877506
DOI: 10.1016/j.str.2017.07.016

実験手法

ELECTRON MICROSCOPY (8 Å)