Ontology highlight
ABSTRACT:
SUBMITTER: Wong JE
PROVIDER: S-EPMC4356369 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Wong Jaslyn E M M JE Midtgaard Søren Roi SR Gysel Kira K Thygesen Mikkel B MB Sørensen Kasper K KK Jensen Knud J KJ Stougaard Jens J Thirup Søren S Blaise Mickaël M
Acta crystallographica. Section D, Biological crystallography 20150226 Pt 3
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 cont ...[more]