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The streptococcal binding site in the gelatin-binding domain of fibronectin is consistent with a non-linear arrangement of modules.

By Kate E Atkin, Andrew S Brentnall, Gemma Harris, Richard Bingham, Michele C Erat, Christopher J Millard, Ulrich Schwarz-Linek, David Staunton, Ioannis Vakonakis, Iain D Campbell and Jennifer R Potts


Fibronectin-binding proteins (FnBPs) of Staphylococcus aureus and Streptococcus pyogenes mediate invasion of human endothelial and epithelial cells in a process likely to aid the persistence and/or dissemination of infection. In addition to binding sites for the N-terminal domain (NTD) of fibronectin (Fn), a number of streptococcal FnBPs also contain an upstream region (UR) that is closely associated with an NTD-binding region; UR binds to the adjacent gelatin-binding domain (GBD) of Fn. Previously, UR was shown to be required for efficient streptococcal invasion of epithelial cells. Here we show, using a Streptococcus zooepidemicus FnBP, that the UR-binding site in GBD resides largely in the (8)F1(9)F1 module pair. We also show that UR inhibits binding of a peptide from the α1 chain of type I collagen to (8)F1(9)F1 and that UR binding to (8)F1 is likely to occur through anti-parallel β-zipper formation. Thus, we propose that streptococcal proteins that contain adjacent NTD- and GBD-binding sites form a highly unusual extended tandem β-zipper that spans the two domains and mediates high affinity binding to Fn through a large intermolecular interface. The proximity of the UR- and NTD-binding sequences in streptococcal FnBPs is consistent with a non-linear arrangement of modules in the tertiary structure of the GBD of Fn

Topics: Q1, QH301
Publisher: The American Society for Biochemistry and Molecular Biology
Year: 2010
OAI identifier: oai:eprints.hud.ac.uk:10020

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  1. (1990). Fibronectins, doi
  2. (2005). Proteins Struct. doi
  3. (2010). Received for publication,
  4. (2002). The PyMOL Molecular Graphics System, DeLano Scientific,
  5. (2002). The PyMOL Molecular Graphics System, DeLano Scientific, Palo Alto,

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