View source for 7w64


==Crystal structure of minor pilin TcpB from Vibrio cholerae complexed with N-terminal peptide fragment of TcpF==
<StructureSection load='7w64' size='340' side='right'caption='[[7w64]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7w64]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W64 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7w64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w64 OCA], [https://pdbe.org/7w64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w64 RCSB], [https://www.ebi.ac.uk/pdbsum/7w64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w64 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TCPB_VIBCH TCPB_VIBCH] Involved in TCP pilus biogenesis.
<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 7w64" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Iida T]]
[[Category: Iimori M]]
[[Category: Imoto Y]]
[[Category: Kawahara K]]
[[Category: Maruno T]]
[[Category: Matsuda S]]
[[Category: Muroga Y]]
[[Category: Nakamura S]]
[[Category: Ohkubo T]]
[[Category: Oki H]]
[[Category: Uchiyama S]]
[[Category: Yoshida A]]
[[Category: Yoshida T]]