Natural Structural Biology
4, 833 - 838 (1997)
doi:10.1038/nsb1097-833
Structure of the collagen-binding domain from a Staphylococcus aureus adhesinJindrich Symersky1, Joseph M. Patti2, Mike Carson1, Karen House-Pompeo2, Michael Teale1, Dwight Moore1, Lei Jin1, Amy Schneider2, Lawrence J. DeLucas1, 3, Magnus Höök2, 4
& Sthanam V.L. Narayana1, 3, 5
1Center for Macromolecular Crystallography, University of Alabama at Birmingham, Birmingham, Alabama 35294,USA.
2Albert B. Alkek Institute of Biosciences and Technology, Center for Extracellular Matrix Biology, Texas A&M University, Houston, Texas 77030, USA.
3School of Optometry, University of Alabama at Birmingham, Birmingham, Alabama 35294, USA.
4Department of Biochemistry, Texas A&M University, Houston, Texas 77030, USA.
5narayana@orion.cmc.uab.edu 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  -sheets and two short  -helices. Triple-helical collagen model probes were used in a systematic docking search to identify the collagen-binding site. A groove on -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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