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| Subject Categories: Cell & Tissue Architecture | Structural Biology |
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| The EMBO Journal
(2005) 24, 4224–4236, doi:10.1038/sj.emboj.7600888 Published online 15 December 2005 |
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| A 'Collagen Hug' Model for Staphylococcus aureus CNA binding to collagen |
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| Yinong Zong1, 4, Yi Xu2, 4, Xiaowen Liang2, Douglas R Keene3, Agneta Höök2, Shivasankarappa Gurusiddappa2, Magnus Höök2 and Sthanam V L Narayana1 |
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1 School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL, USA 2 Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University Health Science Center, Houston, TX, USA 3 Shriners Hospital for Children, Portland, OR, USA To whom correspondence should be addressed Sthanam V L Narayana, Center for Biophysical Sciences and Engineering, School of Optometry, University of Alabama at Birmingham, 1025 18th Street South, Birmingham, AL 35294, USA. Tel.: +1 205 934 0119; Fax: +1 205 975 0538; E-mail: narayana@uab.edu Magnus Höök, Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University Health Science Center, 2121 W. Holcombe Blvd, Houston, TX 77030-3303, USA. Tel.: +1 713 677 7552; Fax: +1 713 677 7576; E-mail: mhook@ibt.tamhsc.edu 4 These authors contributed equally to this work Received 14 June 2005; Accepted 4 November 2005; Published online 15 December 2005. |
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| Abstract |
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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 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  -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. |
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| Keywords: bacterial adhesion, collagen binding, protein–protein, surface proteins |
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