5KUA
Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus
5KUA の概要
| エントリーDOI | 10.2210/pdb5kua/pdb |
| EMDBエントリー | 8287 |
| 分子名称 | pilin (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 | Neisseria meningitidis |
| タンパク質・核酸の鎖数 | 26 |
| 化学式量合計 | 443746.73 |
| 構造登録者 | Kolappan, S.,Coureuil, M.,Yu, X.,Nassif, X.,Craig, L.,Egelman, E.H. (登録日: 2016-07-13, 公開日: 2016-10-12, 最終更新日: 2024-10-16) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (6 Å) |
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