7w65: Difference between revisions

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</table>

== Function ==

[https://www.uniprot.org/uniprot/~~TCPF_VIBC3 TCPF_VIBC3~~] Involved in TCP pilus biogenesis. May be a channel protein (~~By similarity~~).

[https://www.uniprot.org/uniprot/TCPF_VIBCH TCPF_VIBCH] Involved in TCP pilus biogenesis. May be a channel protein.

== Publication Abstract from PubMed ==

Colonization of the host intestine is the most important step in Vibrio cholerae 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 V. cholerae colonization and is a new potential therapeutic target.

Structural basis for the toxin-coregulated pilus-dependent secretion of Vibrio cholerae colonization factor.,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 Sci Adv. 2022 Oct 14;8(41):eabo3013. doi: 10.1126/sciadv.abo3013. Epub 2022 Oct , 14. PMID:36240278<ref>PMID:36240278</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Pilin 3D structures|Pilin 3D structures]]

== References ==

__TOC__

</StructureSection>

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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/TCPF_VIBC3 TCPF_VIBC3] Involved in TCP pilus biogenesis. May be a channel protein (By similarity).
+[https://www.uniprot.org/uniprot/TCPF_VIBCH TCPF_VIBCH] Involved in TCP pilus biogenesis. May be a channel protein.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Colonization of the host intestine is the most important step in Vibrio cholerae 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 V. cholerae colonization and is a new potential therapeutic target.
+Structural basis for the toxin-coregulated pilus-dependent secretion of Vibrio cholerae colonization factor.,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 Sci Adv. 2022 Oct 14;8(41):eabo3013. doi: 10.1126/sciadv.abo3013. Epub 2022 Oct , 14. PMID:36240278<ref>PMID:36240278</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 7w65" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Pilin 3D structures|Pilin 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>