Structural insight into binding of Staphylococcus aureus to human fibronectin

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

doi:10.1016/j.febslet.2005.12.008

Structural insight into binding of Staphylococcus aureus to human fibronectin

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

Biology

Research output: Contribution to journal › Article › peer-review

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 language	English
Pages (from-to)	273-277
Number of pages	5
Journal	FEBS Letters
Volume	580
Issue number	1
DOIs	https://doi.org/10.1016/j.febslet.2005.12.008
Publication status	Published - 9 Jan 2006

Keywords

fibronectin
NMR
Staphylococcus aureus
MODULE PAIR
PROTEIN
ADHERENCE
PROGRAM

Access to Document

10.1016/j.febslet.2005.12.008

Cite this

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title = "Structural insight into binding of Staphylococcus aureus to human fibronectin",

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.",

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T1 - Structural insight into binding of Staphylococcus aureus to human fibronectin

AU - Pilka, E S

AU - Werner, J M

AU - Schwarz-Linek, U

AU - Pickford, A R

AU - Meenan, N A G

AU - Campbell, I D

AU - Potts, J R

PY - 2006/1/9

Y1 - 2006/1/9

N2 - 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.

AB - 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.

KW - fibronectin

KW - NMR

KW - Staphylococcus aureus

KW - MODULE PAIR

KW - PROTEIN

KW - ADHERENCE

KW - PROGRAM

U2 - 10.1016/j.febslet.2005.12.008

DO - 10.1016/j.febslet.2005.12.008

M3 - Article

C2 - 16376343

SN - 0014-5793

VL - 580

SP - 273

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JO - FEBS Letters

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