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Publication Abstract from PubMed
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 beta-strands in the N-terminal alphabeta loop that align with the major beta-strands to form a continuous 7-stranded antiparallel beta-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 alphabeta 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.
NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus.,Xu XF, Tan YW, Lam L, Hackett J, Zhang M, Mok YK J Biol Chem. 2004 Jul 23;279(30):31599-605. Epub 2004 May 24. PMID:15159389[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Xu XF, Tan YW, Lam L, Hackett J, Zhang M, Mok YK. NMR structure of a type IVb pilin from Salmonella typhi and its assembly into pilus. J Biol Chem. 2004 Jul 23;279(30):31599-605. Epub 2004 May 24. PMID:15159389 doi:10.1074/jbc.M404727200
