Structural and Functional Analysis of the Tandem ß-Zipper Interaction of a Streptococcal Protein with Human Fibronectin

Nicole C Norris, Richard J Bingham, Gemma Harris, Adrian Speakman, Richard P O Jones, Andrew Leech, Johan P Turkenburg, Jennifer R Potts

Research output: Contribution to journalArticlepeer-review


Bacterial fibronectin-binding proteins (FnBPs) contain a large intrinsically disordered region (IDR) that mediates adhesion of bacteria to host tissues, and invasion of host cells, through binding to fibronectin (Fn). These FnBP IDRs consist of Fn-binding repeats (FnBRs) that form a highly extended tandem ß-zipper interaction on binding to the N-terminal domain of Fn. Several FnBR residues are highly conserved across bacterial species, and here we investigate their contribution to the interaction. Mutation of these residues to alanine in SfbI-5 (a disordered FnBR from the human pathogen Streptococcus pyogenes) reduced binding, but for each residue the change in free energy of binding was
Original languageEnglish
Pages (from-to)38311-38320
Number of pages10
JournalJournal of Biological Chemistry
Issue number44
Publication statusPublished - 4 Nov 2011

Cite this