3oc5: Difference between revisions

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'''Unreleased structure'''


The entry 3oc5 is ON HOLD  until Paper Publication
==Crystal Structure of the vibrio cholerae secreted colonization factor TcpF==
<StructureSection load='3oc5' size='340' side='right'caption='[[3oc5]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oc5]] is a 1 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=3OC5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OC5 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]] 2.4&#8491;</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=3oc5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oc5 OCA], [https://pdbe.org/3oc5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oc5 RCSB], [https://www.ebi.ac.uk/pdbsum/3oc5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oc5 ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
Vibrio cholerae relies on two main virulence factors-toxin-coregulated pilus (TCP) and cholera toxin-to cause the gastrointestinal disease cholera. TCP is a type IV pilus that mediates bacterial autoagglutination and colonization of the intestine. TCP is encoded by the tcp operon, which also encodes TcpF, a protein of unknown function that is secreted by V. cholerae in a TCP-dependent manner. Although TcpF is not required for TCP biogenesis, a tcpF mutant has a colonization defect in the infant mouse cholera model that is as severe as a pilus mutant. Furthermore, TcpF antisera protect against V. cholerae infection. TcpF has no apparent sequence homology to any known protein. Here, we report the de novo X-ray crystal structure of TcpF and the identification of an epitope that is critical for its function as a colonization factor. A monoclonal antibody recognizing this epitope is protective against V. cholerae challenge and adds to the protection provided by an anti-TcpA antibody. These data suggest that TcpF has a novel function in V. cholerae colonization and define a region crucial for this function.


Authors: Craig, L., Kolappan, S., Yuen, A.S.W.
Crystal Structure of the Vibrio cholerae Colonization Factor TcpF and Identification of a Functional Immunogenic Site.,Megli CJ, Yuen AS, Kolappan S, Richardson MR, Dharmasena MN, Krebs SJ, Taylor RK, Craig L J Mol Biol. 2011 Mar 31. PMID:21440558<ref>PMID:21440558</ref>


Description: Crystal Structure Analysis of TcpF
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oc5" style="background-color:#fffaf0;"></div>


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 22 09:34:07 2010''
==See Also==
*[[Colonization factor antigen|Colonization factor antigen]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Craig L]]
[[Category: Kolappan S]]
[[Category: Yuen ASW]]
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