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

Jindrich Symersky, Joseph M. Patti, Mike Carson, Karen House-Pompeo, Michael Teale, Dwight Moore, Lei Jin, Amy Schneider, Lawrence J. Delucas, Magnus Hook, Sthanam V.L. Narayana

    Research output: Contribution to journalArticlepeer-review

    126 Scopus citations

    Abstract

    The crystal structure of the recombinant 19,000 M, 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 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.

    Original languageEnglish (US)
    Pages (from-to)833-838
    Number of pages6
    JournalNature Structural Biology
    Volume4
    Issue number10
    DOIs
    StatePublished - 1997

    ASJC Scopus subject areas

    • Structural Biology
    • Biochemistry
    • Genetics

    Fingerprint

    Dive into the research topics of 'Structure of the collagen-binding domain from a Staphylococcus aureus adhesin'. Together they form a unique fingerprint.

    Cite this