1Q5F

NMR Structure of Type IVb pilin (PilS) from Salmonella typhi

Summary for 1Q5F

• Entry DOI: 10.2210/pdb1q5f/pdb
• NMR Information: BMRB: 5879
• Descriptor: PilS (1 entity in total)
• Functional Keywords: type ivb pilin, alpha-beta roll, monomer, cell adhesion
• Biological source: Salmonella typhi
• Total number of polymer chains: 1
• Total formula weight: 15842.43

Authors

Xu, X.F.,Tan, Y.W.,Hackett, J.,Zhang, M.,Mok, Y.K. (deposition date: 2003-08-07, release date: 2004-07-27, Last modification date: 2022-03-02)

Primary citation

Xu, X.F.,Tan, Y.W.,Lam, L.,Hackett, J.,Zhang, M.,Mok, Y.K.
NMR Structure of a Type IVb Pilin from Salmonella typhi and Its Assembly into Pilus
J.Biol.Chem., 279:31599-31605, 2004

PubMed 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 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.

PubMed: 15159389
DOI: 10.1074/jbc.M404727200

Experimental method

SOLUTION NMR