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

Nature Structural Biology volume 4, pages 833–838 (1997)Cite this article

Abstract

The crystal structure of the recombinant 19,000 Mr binding domain from the Staphylococcus aureus collagen adhesin has been determined at 2 Å resolution. The domain fold is a jelly-roll, composed of two antiparallel β-sheets and two short α-helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on β-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.

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Authors and Affiliations

  1. Center for Macromolecular Crystallography, University of Alabama at Birmingham, Birmingham, Alabama, 35294, USA

    Jindrich Symersky, Mike Carson, Michael Teale, Dwight Moore, Lei Jin, Lawrence J. DeLucas & Sthanam V.L. Narayana

  2. Albert B. Alkek Institute of Biosciences and Technology, Center for Extracellular Matrix Biology, Texas A&M University, Houston, Texas, 77030, USA

    Joseph M. Patti, Karen House-Pompeo, Amy Schneider & Magnus Höök

  3. School of Optometry, University of Alabama at Birmingham, Birmingham, Alabama, 35294, USA

    Lawrence J. DeLucas & Sthanam V.L. Narayana

  4. Department of Biochemistry, Texas A&M University, Houston, Texas, 77030, USA

    Magnus Höök

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  1. Jindrich Symersky
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Symersky, J., Patti, J., Carson, M. et al. Structure of the collagen-binding domain from a Staphylococcus aureus adhesin. Nat Struct Mol Biol 4, 833–838 (1997). https://doi.org/10.1038/nsb1097-833

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