Structure of the collagen-binding domain from a Staphylococcus aureus adhesin.

abstract

• The crystal structure of the recombinant 19,000 M(r) binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 A resolution. The domain fold is a jelly-roll, composed of two antiparallel beta-sheets and two short alpha-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on beta-sheet I exhibited the best surface complementarity to the collagen probes. This site partially overlaps with the peptide sequence previously shown to be critical for collagen binding. Recombinant proteins containing single amino acid mutations designed to disrupt the surface of the putative binding site exhibited significantly lower affinities for collagen. Here we present a structural perspective for the mode of collagen binding by a bacterial surface protein.

authors

• Hook, Magnus

published proceedings

• Nat Struct Biol

altmetric score

• 6

author list (cited authors)

• Symersky, J., Patti, J. M., Carson, M., House-Pompeo, K., Teale, M., Moore, D., ... Narayana, S. V.

citation count

• 129

complete list of authors

• Symersky, J||Patti, JM||Carson, M||House-Pompeo, K||Teale, M||Moore, D||Jin, L||Schneider, A||DeLucas, LJ||Höök, M||Narayana, SV

publication date

• January 1997

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Adhesins, Bacterial
• Binding Sites
• Cloning, Molecular
• Collagen
• Crystallography, X-Ray
• Escherichia Coli
• Models, Molecular
• Models, Structural
• Protein Folding
• Protein Sorting Signals
• Protein Structure, Secondary
• Recombinant Proteins
• Staphylococcus Aureus

Digital Object Identifier (DOI)

• 10.1038/nsb1097-833

start page

• 833

end page

• 838

volume

• 4

issue

• 10

URL

• http://dx.doi.org/10.1038/nsb1097-833