6NJP
Structure of the assembled ATPase EscN in complex with its central stalk EscO from the enteropathogenic E. coli (EPEC) type III secretion system
6NJP の概要
| エントリーDOI | 10.2210/pdb6njp/pdb |
| EMDBエントリー | 9390 9391 |
| 分子名称 | Translocator EscN, EscO, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| 機能のキーワード | atpase, type iii secretion system, adp, hexamer, hydrolase |
| 由来する生物種 | Escherichia coli O127:H6 (strain E2348/69 / EPEC) 詳細 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 312292.45 |
| 構造登録者 | Majewski, D.D.,Worrall, L.J.,Hong, C.,Atkinson, C.E.,Vuckovic, M.,Watanabe, N.,Yu, Z.,Strynadka, N.C.J. (登録日: 2019-01-03, 公開日: 2019-02-20, 最終更新日: 2024-03-20) |
| 主引用文献 | Majewski, D.D.,Worrall, L.J.,Hong, C.,Atkinson, C.E.,Vuckovic, M.,Watanabe, N.,Yu, Z.,Strynadka, N.C.J. Cryo-EM structure of the homohexameric T3SS ATPase-central stalk complex reveals rotary ATPase-like asymmetry. Nat Commun, 10:626-626, 2019 Cited by PubMed Abstract: Many Gram-negative bacteria, including causative agents of dysentery, plague, and typhoid fever, rely on a type III secretion system - a multi-membrane spanning syringe-like apparatus - for their pathogenicity. The cytosolic ATPase complex of this injectisome is proposed to play an important role in energizing secretion events and substrate recognition. We present the 3.3 Å resolution cryo-EM structure of the enteropathogenic Escherichia coli ATPase EscN in complex with its central stalk EscO. The structure shows an asymmetric pore with different functional states captured in its six catalytic sites, details directly supporting a rotary catalytic mechanism analogous to that of the heterohexameric F/V-ATPases despite its homohexameric nature. Situated at the C-terminal opening of the EscN pore is one molecule of EscO, with primary interaction mediated through an electrostatic interface. The EscN-EscO structure provides significant atomic insights into how the ATPase contributes to type III secretion, including torque generation and binding of chaperone/substrate complexes. PubMed: 30733444DOI: 10.1038/s41467-019-08477-7 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.29 Å) |
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