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|Title:||NMR structure of a Type IVb pilin from Salmonella typhi and its assembly into pilus||Authors:||Xu, X.-F.
|Issue Date:||23-Jul-2004||Citation:||Xu, X.-F., Tan, Y.-W., Lam, L., Hackett, J., Zhang, M., Mok, Y.-K. (2004-07-23). NMR structure of a Type IVb pilin from Salmonella typhi and its assembly into pilus. Journal of Biological Chemistry 279 (30) : 31599-31605. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M404727200||Abstract:||The structure of the N-terminal-truncated Type IVb structural pilin (t-PilS) from Salmonella typhi was determined by NMR. Although topologically similar to the recently determined x-ray structure of pilin from Vibrio cholerae toxin-coregulated pilus, the only Type IVb pilin with known structure, t-PilS contains many distinct structural features. The protein contains an extra pair of β-strands in the N-terminal αβ loop that align with the major β-strands to form a continuous 7-stranded antiparallel β-sheet. The C-terminal disulfide-bonded region of t-PilS is only half the length of that of toxin-coregulated pilus pilin. A model of S. typhi pilus has been proposed and mutagenesis studies suggested that residues on both the αβ loop and the C-terminal disulfide-bonded region of PilS might be involved in binding specificity of the pilus. This model structure reveals an exposed surface between adjacent subunits of PilS that could be a potential binding site for the cystic fibrosis transmembrane conductance regulator.||Source Title:||Journal of Biological Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/101231||ISSN:||00219258||DOI:||10.1074/jbc.M404727200|
|Appears in Collections:||Staff Publications|
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