Structural insight into binding of Staphylococcus aureus to human fibronectin

E. Pilka, J. Werner, U. Schwarz-Linek, Andy Pickford, N. Meenan, I. Campbell, J. Potts

Research output: Contribution to journalArticlepeer-review


Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 modules in the N-terminal domain of Fn is maintained on bacterial peptide binding but there is a small change in the intermodule orientation and alignment of β-strands that are predicted to bind the peptide. The module pair is elongated, as in the unbound state. Combined with evidence that residues in both 4F1 and 5F1 are directly involved in peptide binding, this observation supports the hypothesis that, when bound to intact Fn, the bacterial protein adopts an unusual, highly extended conformation.
Original languageEnglish
Pages (from-to)273-277
Number of pages5
JournalFEBS Letters
Issue number1
Publication statusPublished - 2006


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