3OC5

Crystal Structure of the vibrio cholerae secreted colonization factor TcpF

Summary for 3OC5

• Entry DOI: 10.2210/pdb3oc5/pdb
• Related: 3OC8
• Descriptor: Toxin coregulated pilus biosynthesis protein F (2 entities in total)
• Functional Keywords: multidomain protein, immunoglobulin-like (ig-like) fold, cell adhesion
• Biological source: Vibrio cholerae
• Cellular location: Cell outer membrane; Peripheral membrane protein (Potential): P0C6Q5
• Total number of polymer chains: 1
• Total formula weight: 35882.94

Authors

Craig, L.,Kolappan, S.,Yuen, A.S.W. (deposition date: 2010-08-09, release date: 2011-04-20, Last modification date: 2024-10-30)

Primary citation

Megli, 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

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)