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

The crystal and solution structures of the T. thermophilus NlpC/P60 d, l-endopeptidase as well as the co-crystal structure of its N-terminal LysM domains bound to chitohexaose allow a proposal to be made regarding how the enzyme recognizes peptidoglycan. 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.
Authors:
 [1] ;  [2] ;  [1] ; ; ;  [3] ; ; ;  [1]
  1. Aarhus University, Gustav Wieds Vej 10C, 8000 Aarhus (Denmark)
  2. University of Copenhagen, Universitetsparken 5, 2100 Copenhagen (Denmark)
  3. University of Copenhagen, Thorvaldsensvej 40, 1871 Frederiksberg C (Denmark)
Publication Date:
OSTI Identifier:
22347724
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section D: Biological Crystallography; Journal Volume: 71; Journal Issue: Pt 3; Other Information: PMCID: PMC4356369; PMID: 25760608; PUBLISHER-ID: rr5089; OAI: oai:pubmedcentral.nih.gov:4356369; Copyright (c) Wong et al. 2015; This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
Denmark
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; CRYSTALS; DIMERIZATION; INTERACTIONS; LIGANDS; MATHEMATICAL SOLUTIONS; RESOLUTION; SCATTERING; SOLUTIONS; SUBSTRATES