7VNJ

Complex structure of Clostridioides difficile enzymatic component (CDTa) and binding component (CDTb) pore with short stem

7VNJ の概要

• エントリーDOI: 10.2210/pdb7vnj/pdb
• EMDBエントリー: 32041
• 分子名称: ADP-ribosylating binary toxin binding subunit CdtB, ADP-ribosyltransferase enzymatic component, CALCIUM ION (3 entities in total)
• 機能のキーワード: complex, translocation, oligomer, unfoldase, toxin
• 由来する生物種: Clostridioides difficile; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 579862.09

構造登録者

Yamada, T.,Kawamoto, A.,Yoshida, T.,Sato, Y.,Kato, T.,Tsuge, H. (登録日: 2021-10-11, 公開日: 2022-10-26, 最終更新日: 2024-06-19)

主引用文献

Kawamoto, A.,Yamada, T.,Yoshida, T.,Sato, Y.,Kato, T.,Tsuge, H.
Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.
Nat Commun, 13:6119-6119, 2022

PubMed Abstract: Some bacteria express a binary toxin translocation system, consisting of an enzymatic subunit and translocation pore, that delivers enzymes into host cells through endocytosis. The most clinically important bacterium with such a system is Clostridioides difficile (formerly Clostridium). The CDTa and CDTb proteins from its system represent important therapeutic targets. CDTb has been proposed to be a di-heptamer, but its physiological heptameric structure has not yet been reported. Here, we report the cryo-EM structure of CDTa bound to the CDTb-pore, which reveals that CDTa binding induces partial unfolding and tilting of the first CDTa α-helix. In the CDTb-pore, an NSS-loop exists in 'in' and 'out' conformations, suggesting its involvement in substrate translocation. Finally, 3D variability analysis revealed CDTa movements from a folded to an unfolded state. These dynamic structural information provide insights into drug design against hypervirulent C. difficile strains.

PubMed: 36253419
DOI: 10.1038/s41467-022-33888-4

実験手法

ELECTRON MICROSCOPY (2.56 Å)