7W63

Crystal structure of minor pilin TcpB from Vibrio cholerae

Summary for 7W63

• Entry DOI: 10.2210/pdb7w63/pdb
• Descriptor: Toxin-coregulated pilus biosynthesis protein B, SULFATE ION (3 entities in total)
• Functional Keywords: type ivb pilus, vibrio cholerae, minor pilin., cell adhesion
• Biological source: Vibrio cholerae
• Total number of polymer chains: 3
• Total formula weight: 133788.04

Authors

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. (deposition date: 2021-12-01, release date: 2022-11-09, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.32 Å)