An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase

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  • Jaslyn E M M Wong
  • Søren Roi Midtgaard, Niels Bohr Institute, Faculty of Science, University of Copenhagen, Denmark
  • Kira Gysel
  • Mikkel B Thygesen, Centre for Carbohydrate Recognition and Signalling, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Kasper K Sørensen, Centre for Carbohydrate Recognition and Signalling, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Knud J Jensen, Centre for Carbohydrate Recognition and Signalling, Department of Chemistry, Faculty of Science, University of Copenhagen, Denmark
  • Jens Stougaard
  • Søren Thirup
  • Mickaël Blaise, Denmark

LysM domains, which are frequently present as repetitive entities in both bacterial and plant proteins, are known to interact with carbohydrates containing N-acetylglucosamine (GlcNAc) moieties, such as chitin and peptidoglycan. In bacteria, the functional significance of the involvement of multiple LysM domains in substrate binding has so far lacked support from high-resolution structures of ligand-bound complexes. Here, a structural study of the Thermus thermophilus NlpC/P60 endopeptidase containing two LysM domains is presented. The crystal structure and small-angle X-ray scattering solution studies of this endopeptidase revealed the presence of a homodimer. The structure of the two LysM domains co-crystallized with N-acetyl-chitohexaose revealed a new intermolecular binding mode that may explain the differential interaction between LysM domains and short or long chitin oligomers. By combining the structural information with the three-dimensional model of peptidoglycan, a model suggesting how protein dimerization enhances the recognition of peptidoglycan is proposed.

Original languageEnglish
JournalActa crystallographica Section D: Structural biology
Volume71
IssuePt 3
Pages (from-to)592-605
Number of pages14
ISSN2059-7983
DOIs
Publication statusPublished - Mar 2015

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