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

Richard J. Bingham, Enrique Rudiño-Piñera, Nicola A G Meenan, Ulrich Schwarz-Linek, Johan P. Turkenburg, Magnus Höök, Elspeth F. Garman, Jennifer R. Potts

Research output: Contribution to journalArticle

92 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 ≈40-residue FnBR forms antiparallel strands along the triple-stranded β-sheets of four sequential F1 modules ( 2-5F1) with each FnBR/2-5F1 interface burying a total surface area of ≈4,300 Å2. 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.

LanguageEnglish
Pages12254-12258
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
Externally publishedYes

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Fibronectins
Staphylococcus aureus
Binding Sites
Protein S
Streptococcus pyogenes
Cell Wall
Endothelial Cells
Proteins

Cite this

Bingham, Richard J. ; Rudiño-Piñera, Enrique ; Meenan, Nicola A G ; Schwarz-Linek, Ulrich ; Turkenburg, Johan P. ; Höök, Magnus ; Garman, Elspeth F. ; Potts, Jennifer R. / Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains. In: Proceedings of the National Academy of Sciences of the United States of America. 2008 ; Vol. 105, No. 34. pp. 12254-12258.
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Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains. / Bingham, Richard J.; Rudiño-Piñera, Enrique; Meenan, Nicola A G; Schwarz-Linek, Ulrich; Turkenburg, Johan P.; Höök, Magnus; Garman, Elspeth F.; Potts, Jennifer R.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 105, No. 34, 26.08.2008, p. 12254-12258.

Research output: Contribution to journalArticle

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T1 - Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains

AU - Bingham, Richard J.

AU - Rudiño-Piñera, Enrique

AU - Meenan, Nicola A G

AU - Schwarz-Linek, Ulrich

AU - Turkenburg, Johan P.

AU - Höök, Magnus

AU - Garman, Elspeth F.

AU - Potts, Jennifer R.

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N2 - 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 ≈40-residue FnBR forms antiparallel strands along the triple-stranded β-sheets of four sequential F1 modules ( 2-5F1) with each FnBR/2-5F1 interface burying a total surface area of ≈4,300 Å2. 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.

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KW - Host-pathogen interaction

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