Vibrio cholerae colonization factor TcpF: Difference between revisions
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By looking the X-ray crystal structure of native TcpF, the structure of TcpF is consisted with an <scene name='Vibrio_cholerae_colonization_factor_TcpF/N_terminal_domain/1'>N terminal domain (NTD;residues | By looking the X-ray crystal structure of native TcpF, the structure of TcpF is consisted with an <scene name='Vibrio_cholerae_colonization_factor_TcpF/N_terminal_domain/1'>N terminal domain (NTD;residues 1 to 185)</scene> and a C-terminal domain (CTD; residues 190–318) connected by an extended linker segment (residues 186–189). In detail, the NTD is composed of a short twisted β-sheet encapsulated by seven short α-helices with a second twisted β-sheet forming the floor of this domain. The NTD is connected with The CTD, which consists of two twisted antiparallel β-sheets. | ||
Revision as of 20:43, 4 May 2012
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IntroductionIntroduction
Molecule: Toxin coregulated pilus biosynthesis protein F
Type:protein Length: 318 Organism:Vibrio Cholerae
TcpF is a toxin-coregulated pilus that facilitates colonization of vibrio cholerae in the intestine. 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. TcpF is secreted from bacterial cell by the TCP apparatus and is also essential for colonization.
StructureStructure
By looking the X-ray crystal structure of native TcpF, the structure of TcpF is consisted with an and a C-terminal domain (CTD; residues 190–318) connected by an extended linker segment (residues 186–189). In detail, the NTD is composed of a short twisted β-sheet encapsulated by seven short α-helices with a second twisted β-sheet forming the floor of this domain. The NTD is connected with The CTD, which consists of two twisted antiparallel β-sheets.
FunctionFunction
TcpF, identified in classical isolates of V. cholerae O1 is an essential factor for colonization in the infant mouse cholera model. Bacteria lacking tcpF are deficient in colonization, and anti-TcpF antibodies are protective in the infant mouse cholera model. TcpF is expressed in vivo during human infection and generates a substantial immune response in patients infected with V. cholera. The mechanism for the action of TcpF remains to be elucidated.
ApplicationApplication
