Journal
EMBO JOURNAL
Volume 24, Issue 24, Pages 4224-4236Publisher
WILEY
DOI: 10.1038/sj.emboj.7600888
Keywords
bacterial adhesion; collagen binding; protein-protein; surface proteins
Categories
Funding
- NIAID NIH HHS [R21 AI061555, AI061555, R01 AI064815, R56 AI020624, AI064815, R01 AI020624, AI20624] Funding Source: Medline
- NIAMS NIH HHS [AR44415, R01 AR044415] Funding Source: Medline
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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 apoprotein 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 inter-domain interactions and by the N2 C-terminal extension that complements a P-sheet on NI. 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.
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