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Structural insight into binding of Staphylococcus aureus to human fibronectin

Record type: Article

Staphylococcus aureus possesses cell-wall attached proteins that bind the human protein fibronectin (Fn). An intermodule interface between the 4F1 and 5F1 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 ?-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 4F1 and 5F1 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.

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Citation

Pilka, Ewa S., Werner, Joern M., Schwarz-Linek, Ulrich, Pickford, Andrew R., Meenan, Nicola A.G., Campbell, Iain D. and Potts, Jennifer R. (2006) Structural insight into binding of Staphylococcus aureus to human fibronectin Febs Letters, 580, (1), pp. 273-277. (doi:10.1016/j.febslet.2005.12.008).

More information

Submitted date: 10 October 2005
Published date: 9 January 2006
Keywords: fibronectin, nmr, Staphylococcus aureus

Identifiers

Local EPrints ID: 56614
URI: http://eprints.soton.ac.uk/id/eprint/56614
ISSN: 0014-5793
PURE UUID: 49a01ccd-666c-4a1f-89e6-5d4760b41be6
ORCID for Joern M. Werner: ORCID iD orcid.org/0000-0002-4712-1833

Catalogue record

Date deposited: 07 Aug 2008
Last modified: 17 Jul 2017 14:30

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Contributors

Author: Ewa S. Pilka
Author: Joern M. Werner ORCID iD
Author: Ulrich Schwarz-Linek
Author: Andrew R. Pickford
Author: Nicola A.G. Meenan
Author: Iain D. Campbell
Author: Jennifer R. Potts

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