A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. uri icon

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 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.

published proceedings

  • EMBO J

altmetric score

  • 7

author list (cited authors)

  • Zong, Y., Xu, Y. i., Liang, X., Keene, D. R., Hk, A., Gurusiddappa, S., Hk, M., & Narayana, S.

citation count

  • 180
  • 196

complete list of authors

  • Zong, Yinong||Xu, Yi||Liang, Xiaowen||Keene, Douglas R||Höök, Agneta||Gurusiddappa, Shivasankarappa||Höök, Magnus||Narayana, Sthanam VL

publication date

  • December 2005

publisher