Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Wong JE 

PROVIDER: S-EPMC4356369 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

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]

Similar Datasets

| S-EPMC4083421 | biostudies-literature
| S-EPMC1994126 | biostudies-other
| S-EPMC2667722 | biostudies-literature
| S-EPMC4392113 | biostudies-literature
| S-EPMC3210742 | biostudies-literature
| S-EPMC9614474 | biostudies-literature
| S-EPMC1150177 | biostudies-other
| S-EPMC3097085 | biostudies-literature
| S-EPMC2898448 | biostudies-literature
| S-EPMC5626579 | biostudies-literature