The structural basis for the association of eukaryotic and prokaryotic protein receptors and their triple-helical collagen ligand remains poorly understood. Here, we present the crystal structures of a high affinity subsegment of the Staphylococcus aureus collagen-binding CNA as an apo-protein and in complex with a synthetic collagen-like triple helical peptide. The apo-protein structure is composed of two subdomains (N1 and N2), each adopting a variant IgG-fold, and a long linker that connects N1 and N2. The structure is stabilized by hydrophobic interdomain interactions and by the N2 C-terminal extension that complements a β-sheet on N1. In the ligand complex, the collagen-like peptide penetrates through a spherical hole formed by the two subdomains and the N1-N2 linker. Based on these two structures we propose a dynamic, multistep binding model, called the 'Collagen Hug' that is uniquely designed to allow multidomain collagen binding proteins to bind their extended rope-like ligand. © 2005 European Molecular Biology Organization | All Rights Reserved.
CITATION STYLE
Zong, Y., Xu, Y., Liang, X., Keene, D. R., Höök, A., Gurusiddappa, S., … Narayana, S. V. L. (2005). A “Collagen Hug” Model for Staphylococcus aureus CNA binding to collagen. EMBO Journal, 24(24), 4224–4236. https://doi.org/10.1038/sj.emboj.7600888
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