7W65

Crystal structure of minor pilin TcpB from Vibrio cholerae complexed with secreted protein TcpF

7W65 の概要

• エントリーDOI: 10.2210/pdb7w65/pdb
• 分子名称: Toxin-coregulated pilus biosynthesis protein B, Toxin coregulated pilus biosynthesis protein F (2 entities in total)
• 機能のキーワード: type ivb pilus, vibrio cholerae, minor pilin., cell adhesion
• 由来する生物種: Vibrio cholerae; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 238170.72

構造登録者

Oki, H.,Kawahara, K.,Iimori, M.,Imoto, Y.,Maruno, T.,Uchiyama, S.,Muroga, Y.,Yoshida, A.,Yoshida, T.,Ohkubo, T.,Matsuda, S.,Iida, T.,Nakamura, S. (登録日: 2021-12-01, 公開日: 2022-11-09, 最終更新日: 2023-11-29)

主引用文献

Oki, H.,Kawahara, K.,Iimori, M.,Imoto, Y.,Nishiumi, H.,Maruno, T.,Uchiyama, S.,Muroga, Y.,Yoshida, A.,Yoshida, T.,Ohkubo, T.,Matsuda, S.,Iida, T.,Nakamura, S.
Structural basis for the toxin-coregulated pilus-dependent secretion of Vibrio cholerae colonization factor.
Sci Adv, 8:eabo3013-eabo3013, 2022

PubMed Abstract: Colonization of the host intestine is the most important step in infection. The toxin-coregulated pilus (TCP), an operon-encoded type IVb pilus (T4bP), plays a crucial role in this process, which requires an additional secreted protein, TcpF, encoded on the same TCP operon; however, its mechanisms of secretion and function remain elusive. Here, we demonstrated that TcpF interacts with the minor pilin, TcpB, of TCP and elucidated the crystal structures of TcpB alone and in complex with TcpF. The structural analyses reveal how TCP recognizes TcpF and its secretory mechanism via TcpB-dependent pilus elongation and retraction. Upon binding to TCP, TcpF forms a flower-shaped homotrimer with its flexible N terminus hooked onto the trimeric interface of TcpB. Thus, the interaction between the minor pilin and the N terminus of the secreted protein, namely, the T4bP secretion signal, is key for colonization and is a new potential therapeutic target.

PubMed: 36240278
DOI: 10.1126/sciadv.abo3013

実験手法

X-RAY DIFFRACTION (4.05 Å)