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1Q5F

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

Summary for 1Q5F
Entry DOI10.2210/pdb1q5f/pdb
NMR InformationBMRB: 5879
DescriptorPilS (1 entity in total)
Functional Keywordstype ivb pilin, alpha-beta roll, monomer, cell adhesion
Biological sourceSalmonella typhi
Total number of polymer chains1
Total formula weight15842.43
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: 2024-11-13)
Primary citationXu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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