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7W65

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

Summary for 7W65
Entry DOI10.2210/pdb7w65/pdb
DescriptorToxin-coregulated pilus biosynthesis protein B, Toxin coregulated pilus biosynthesis protein F (2 entities in total)
Functional Keywordstype ivb pilus, vibrio cholerae, minor pilin., cell adhesion
Biological sourceVibrio cholerae
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Total number of polymer chains6
Total formula weight238170.72
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: 2023-11-29)
Primary citationOki, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.05 Å)
Structure validation

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