By the same authors

From the same journal

Structural insight into binding of Staphylococcus aureus to human fibronectin

Research output: Contribution to journalArticle

Published copy (DOI)

Author(s)

  • E S Pilka
  • J M Werner
  • U Schwarz-Linek
  • A R Pickford
  • N A G Meenan
  • I D Campbell
  • J R Potts

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 9 Jan 2006
Issue number1
Volume580
Number of pages5
Pages (from-to)273-277
Original languageEnglish

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.

    Research areas

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

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