1o9a
From Proteopedia
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SOLUTION STRUCTURE OF THE COMPLEX OF 1F12F1 FROM FIBRONECTIN WITH B3 FROM FNBB FROM S. DYSGALACTIAE
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Ehlers-Danlos syndrome, type X, 225310 (1) OMIM:[135600]
About this Structure
1O9A is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Mon Nov 12 18:30:54 2007
