1O9A: Solution structure of the complex of 1F12F1 from fibronectin with B3 from FnBB from S. dysgalactiae

Citation:
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.
PDB ID: 1O9ADownload
MMDB ID: 23069
PDB Deposition Date: 2002/12/11
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Homo sapiens
Similar Structures:
Biological Unit for 1O9A: dimeric; determined by software (PISA)
Molecular Components in 1O9A
Label Count Molecule
Proteins (2 molecules)
1
Fibronectin(Gene symbol: FN1)
Molecule annotation
1
Fibronectin Binding Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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