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3OC8

Crystal Structure of the C-terminal Domain of the Vibrio cholerae soluble colonization factor TcpF

Summary for 3OC8
Entry DOI10.2210/pdb3oc8/pdb
Related3OC5
DescriptorToxin coregulated pilus biosynthesis protein F, 1,4-DIETHYLENE DIOXIDE, GLYCEROL, ... (5 entities in total)
Functional Keywordsimmunoglobulin-like fold, cell adhesion
Biological sourceVibrio cholerae
Cellular locationCell outer membrane; Peripheral membrane protein (Potential): P0C6Q5
Total number of polymer chains1
Total formula weight16065.98
Authors
Craig, L.,Kolappan, S.,Yuen, A.S.W. (deposition date: 2010-08-09, release date: 2011-04-20, Last modification date: 2023-09-06)
Primary citationMegli, C.J.,Yuen, A.S.,Kolappan, S.,Richardson, M.R.,Dharmasena, M.N.,Krebs, S.J.,Taylor, R.K.,Craig, L.
Crystal Structure of the Vibrio cholerae Colonization Factor TcpF and Identification of a Functional Immunogenic Site.
J.Mol.Biol., 409:146-158, 2011
Cited by
PubMed Abstract: 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.
PubMed: 21440558
DOI: 10.1016/j.jmb.2011.03.027
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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