1o9a
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SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this StructureAbout this Structure
1O9A is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper., Schwarz-Linek U, Werner JM, Pickford AR, Gurusiddappa S, Kim JH, Pilka ES, Briggs JA, Gough TS, Hook M, Campbell ID, Potts JR, Nature. 2003 May 8;423(6936):177-81. PMID:12736686
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