1O9A

Solution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae

Summary for 1O9A

• Entry DOI: 10.2210/pdb1o9a/pdb
• Related: 1E88 1E8B 1FBR 1FNA 1FNF 1FNH 1J8K 1QGB 1QO6 1TTF 1TTG 2FN2
• Descriptor: FIBRONECTIN, FIBRONECTIN BINDING PROTEIN (2 entities in total)
• Functional Keywords: cell adhesion-complex, host-pathogen protein complex, cell adhesion, fibronectin
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Secreted, extracellular space, extracellular matrix: P02751
• Total number of polymer chains: 2
• Total formula weight: 14603.93

Authors

Schwarz-Linek, U.,Werner, J.M.,Pickford, A.R.,Pilka, E.S.,Gurusiddappa, S.,Briggs, J.A.G.,Hook, M.,Campbell, I.D.,Potts, J.R. (deposition date: 2002-12-11, release date: 2003-05-08, Last modification date: 2024-11-20)

Primary citation

Schwarz-Linek, U.,Werner, J.M.,Pickford, A.R.,Gurusiddappa, S.,Kim, J.H.,Pilka, E.S.,Briggs, J.A.,Gough, T.S.,Hook, M.,Campbell, I.D.,Potts, J.R.
Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper.
Nature, 423:177-181, 2003

PubMed Abstract: Staphylococcus aureus and Streptococcus pyogenes, two important human pathogens, target host fibronectin (Fn) in their adhesion to and invasion of host cells. Fibronectin-binding proteins (FnBPs), anchored in the bacterial cell wall, have multiple Fn-binding repeats in an unfolded region of the protein. The bacterium-binding site in the amino-terminal domain (1-5F1) of Fn contains five sequential Fn type 1 (F1) modules. Here we show the structure of a streptococcal (S. dysgalactiae) FnBP peptide (B3) in complex with the module pair 1F12F1. This identifies 1F1- and 2F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules-the first example of a tandem beta-zipper. Sequence analyses of larger regions of FnBPs from S. pyogenes and S. aureus reveal a repeating pattern of F1-binding motifs that match the pattern of F1 modules in 1-5F1 of Fn. In the process of Fn-mediated invasion of host cells, therefore, the bacterial proteins seem to exploit the modular structure of Fn by forming extended tandem beta-zippers. This work is a vital step forward in explaining the full mechanism of the integrin-dependent FnBP-mediated invasion of host cells.

PubMed: 12736686
DOI: 10.1038/nature01589

Experimental method

SOLUTION NMR