2F68

Crystal structure of collagen adhesin (CNA) from S. aureus

Summary for 2F68

• Entry DOI: 10.2210/pdb2f68/pdb
• Descriptor: Collagen adhesin (2 entities in total)
• Functional Keywords: beta barrel, domain swap, cell adhesion
• Biological source: Staphylococcus aureus
• Cellular location: Secreted, cell wall ; Peptidoglycan-anchor : Q53654
• Total number of polymer chains: 1
• Total formula weight: 34388.71

Authors

Zong, Y.,Narayana, S.V.L. (deposition date: 2005-11-28, release date: 2006-12-12, Last modification date: 2024-02-14)

Primary citation

Zong, Y.,Xu, Y.,Liang, X.,Keene, D.R.,Hook, A.,Gurusiddappa, S.,Hook, M.,Narayana, S.V.
A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen.
Embo J., 24:4224-4236, 2005

PubMed 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.

PubMed: 16362049
DOI: 10.1038/sj.emboj.7600888

Experimental method

X-RAY DIFFRACTION (1.95 Å)