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A ‘Collagen Hug’ Model for Staphylococcus aureus CNA binding to collagen
Author(s) -
Zong Yig,
Xu Yi,
Liang Xiaowen,
Keene Douglas R,
Höök Agneta,
Gurusiddappa Shivasankarappa,
Höök Magnus,
Narayana Sthanam V L
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600888
Subject(s) - linker , ligand (biochemistry) , peptide , plasma protein binding , staphylococcus aureus , biology , protein structure , peptide sequence , biophysics , binding site , receptor , biochemistry , genetics , bacteria , computer science , gene , operating system
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 β‐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.