Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains

RJ Bingham, E Rudino-Pinera, NAG Meenan, Ulrich Schwarz-Linek, JP Turkenburg, M Hook, EF Garman, JR Potts

Research output: Contribution to journalArticlepeer-review

115 Citations (Scopus)

Abstract

Staphylococcus aureus can adhere to and invade endothelial cells by binding to the human protein fibronectin (Fn). FnBPA and FnBPB, cell wall-attached proteins from S. aureus, have multiple, intrinsically disordered, high-affinity binding repeats (FnBRs) for Fn. Here, 30 years after the first report of S. aureus/Fn interactions, we present four crystal structures that together comprise the structures of two complete FnBRs, each in complex with four of the N-terminal modules of Fn. Each approximate to 40-residue FnBR forms antiparallel strands along the triple-stranded beta-sheets of four sequential F1 modules ((2-5)F1) with each FnBR/(2-5)F1 interface burying a total surface area of approximate to 4,300 angstrom(2). The structures reveal the roles of residues conserved between S. aureus and Streptococcus pyogenes FnBRs and show that there are few linker residues between FnBRs. The ability to form large intermolecular interfaces with relatively few residues has been proposed to be a feature of disordered proteins, and S. aureus/Fn interactions provide an unusual illustration of this efficiency.
Original languageEnglish
Pages (from-to)12254-12258
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume105
Issue number34
DOIs
Publication statusPublished - 26 Aug 2008

Keywords

  • intrinsic disorder
  • tandem beta-zipper
  • host-pathogen interaction
  • TANDEM BETA-ZIPPER
  • HUMAN ENDOTHELIAL-CELLS
  • DISORDERED PROTEINS
  • EXPERIMENTAL ENDOCARDITIS
  • AFFINITY
  • STREPTOCOCCI
  • RECOGNITION
  • INFECTIONS

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