3FHV

Structural basis of Salmonella typhi type IVb PilS and cystic fibrosis transmembrane conductance regulator (CFTR) interaction

Summary for 3FHV

• Entry DOI: 10.2210/pdb3fhv/pdb
• Related: 3FHU
• Descriptor: Prepilin, cftr peptide (3 entities in total)
• Functional Keywords: pils complex, cftr, cell adhesion-membrane protein complex, cell adhesion/membrane protein
• Biological source: Salmonella typhi; More
• Total number of polymer chains: 3
• Total formula weight: 32939.13

Authors

Balakrishna, A.M.,Swaminathan, K. (deposition date: 2008-12-10, release date: 2009-10-27, Last modification date: 2024-10-30)

Primary citation

Balakrishna, A.M.,Saxena, A.M.,Mok, H.Y.,Swaminathan, K.
Structural basis of typhoid: Salmonella typhi type IVb pilin (PilS) and cystic fibrosis transmembrane conductance regulator interaction.
Proteins, 77:253-261, 2009

PubMed Abstract: The type IVb pilus of the enteropathogenic bacteria Salmonella typhi is a major adhesion factor during the entry of this pathogen into gastrointestinal epithelial cells. Its target of adhesion is a stretch of 10 residues from the first extracellular domain of cystic fibrosis transmembrane conductance regulator (CFTR). The crystal structure of the N-terminal 25 amino acid deleted S. typhi native PilS protein (DeltaPilS), which makes the pilus, was determined at 1.9 A resolution by the multiwavelength anomalous dispersion method. Also, the structure of the complex of DeltaPilS and a target CFTR peptide, determined at 1.8 A, confirms that residues 113-117 (NKEER) of CFTR are involved in binding with the pilin protein and gives us insight on the amino acids that are essential for binding. Furthermore, we have also explored the role of a conserved disulfide bridge in pilus formation. The subunit structure and assembly architecture are crucial for understanding pilus functions and designing suitable therapeutics against typhoid.

PubMed: 19626704
DOI: 10.1002/prot.22500

Experimental method

X-RAY DIFFRACTION (1.9 Å)