Structural highlights
Function
[CNA_STAAU] Mediates attachment of staphylococcal cells to collagen-containing substrata.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen.,Zong Y, Xu Y, Liang X, Keene DR, Hook A, Gurusiddappa S, Hook M, Narayana SV EMBO J. 2005 Dec 21;24(24):4224-36. Epub 2005 Dec 15. PMID:16362049[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zong Y, Xu Y, Liang X, Keene DR, Hook A, Gurusiddappa S, Hook M, Narayana SV. A 'Collagen Hug' model for Staphylococcus aureus CNA binding to collagen. EMBO J. 2005 Dec 21;24(24):4224-36. Epub 2005 Dec 15. PMID:16362049
