Structural insight into binding of Staphylococcus aureus to human fibronectin.
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 beta-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.
Pilka
Ewa S
ES
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.
Werner
Joern M
JM
Schwarz-Linek
Ulrich
U
Pickford
Andrew R
AR
Meenan
Nicola A G
NA
Campbell
Iain D
ID
Potts
Jennifer R
JR
D018829:Adhesins, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding / Q000235:genetics; D017433:Protein Structure, Secondary; D013211:Staphylococcus aureus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013329:Structure-Activity Relationship
D018829:Adhesins, Bacterial; D005353:Fibronectins; D010455:Peptides; C078635:fibronectin-binding proteins, bacterial