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Structural insight into binding of Staphylococcus aureus to human fibronectin
Author(s) -
Pilka Ewa S.,
Werner Joern M.,
Schwarz-Linek Ulrich,
Pickford Andrew R.,
Meenan Nicola A.G.,
Campbell Iain D.,
Potts Jennifer R.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.008
Subject(s) - staphylococcus aureus , peptide , fibronectin , chemistry , biophysics , protein a , plasma protein binding , binding domain , cell wall , biochemistry , cell , bacteria , microbiology and biotechnology , binding site , biology , genetics , antibody , immunology
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 β‐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.