An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. (1st March 2015)

• Record Type: Journal Article
• Authors: Wong, Jaslyn E. M. M.; Midtgaard, Søren Roi; Gysel, Kira; Thygesen, Mikkel B.; Sørensen, Kasper K.; Jensen, Knud J.; Stougaard, Jens; Thirup, Søren; Blaise, Mickaël
• Is Part Of: Acta crystallographica. Volume 71:Part 3(2015:Mar.)
• Page Start: 592
• Page End: 605
• Publication Date: 2015-03-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S139900471402793X
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>LysM domains, which are frequently present as repetitive entities in both bacterial and plant proteins, are known to interact with carbohydrates containing <italic>N</italic>‐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 <italic>Thermus thermophilus</italic> 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 <italic>N</italic>‐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.</p> </abstract>