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  • The EMBO Journal (2005) 24, 4224 - 4236
  • doi:10.1038/sj.emboj.7600888

Published online: 15 December 2005

A 'Collagen Hug' Model for Staphylococcus aureus CNA binding to collagen

Yinong Zong1,a, Yi Xu2,a, Xiaowen Liang2, Douglas R Keene3, Agneta Höök2, Shivasankarappa Gurusiddappa2, Magnus Höök2 and Sthanam V L Narayana1

  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

Correspondence to:

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

aThese authors contributed equally to this work

Received 14 June 2005; Accepted 4 November 2005

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.

  • Keywords:

    • bacterial adhesion,
    • collagen binding,
    • protein–protein,
    • surface proteins