2f68
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(New page: 200px<br /><applet load="2f68" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f68, resolution 1.95Å" /> '''Crystal structure of...)
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Revision as of 08:15, 21 November 2007
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Crystal structure of collagen adhesin (CNA) from S. aureus
Overview
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 inter-domain, interactions and by the N2 C-terminal extension that complements a, beta-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.
About this Structure
2F68 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen., Zong Y, Xu Y, Liang X, Keene DR, Hook A, Gurusiddappa S, Hook M, Narayana SV, EMBO J. 2005 Dec 21;24(24):4224-36. Epub 2005 Dec 15. PMID:16362049
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