Article
- The EMBO Journal (2005) 24, 4224 - 4236
- doi:10.1038/sj.emboj.7600888
Published online: 15 December 2005
Subject Categories:
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
- School of Optometry and Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL, USA
- Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University Health Science Center, Houston, TX, USA
- 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
Abstract
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.
Keywords:
- bacterial adhesion,
- collagen binding,
- protein–protein,
- surface proteins



