Structural insight into binding of Staphylococcus aureus to human fibronectin.

ES Pilka, JM Werner, Ulrich Schwarz-Linek, AR Pickford, NA Meenan, ID Campbell, JR Potts

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the (4)F1 and (5)F1 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 P-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 (4)F1 and (5)F1 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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Original languageEnglish
Pages (from-to)273-277
Number of pages5
JournalFEBS Letters
Volume580
DOIs
Publication statusPublished - 9 Jan 2006

Keywords

  • fibronectin
  • NMR
  • Staphylococcus aureus
  • MODULE PAIR
  • PROTEIN
  • ADHERENCE
  • PROGRAM

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