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5KUA

Cryo-EM reconstruction of Neisseria meningitidis Type IV pilus

5KUA の概要
エントリーDOI10.2210/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: 27698424
DOI: 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)
構造検証レポート
Validation report summary of 5kua
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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