An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
- An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase
Forlagets udgivne version, 2,83 MB, PDF-dokument
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.
|Tidsskrift||Acta Crystallographica. Section D: Biological Crystallography|
|Status||Udgivet - 2015|
Antal downloads er baseret på statistik fra Google Scholar og www.ku.dk