An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase
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An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. / Wong, Mei Mei Jaslyn Elizabeth; Midtgaard, Søren Roi; Gysel, Kira; Thygesen, Mikkel Boas; Sørensen, Kasper Kildegaard; Jensen, Knud Jørgen; Stougaard, Jens; Thirup, Søren Skou; Blaise, Mickael.
I: Acta Crystallographica. Section D: Biological Crystallography, Bind 71, 2015, s. 592-605.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase
AU - Wong, Mei Mei Jaslyn Elizabeth
AU - Midtgaard, Søren Roi
AU - Gysel, Kira
AU - Thygesen, Mikkel Boas
AU - Sørensen, Kasper Kildegaard
AU - Jensen, Knud Jørgen
AU - Stougaard, Jens
AU - Thirup, Søren Skou
AU - Blaise, Mickael
N1 - OA
PY - 2015
Y1 - 2015
N2 - 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.
AB - 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.
U2 - 10.1107/S139900471402793X
DO - 10.1107/S139900471402793X
M3 - Journal article
C2 - 25760608
VL - 71
SP - 592
EP - 605
JO - Acta Crystallographica Section D: Structural Biology
JF - Acta Crystallographica Section D: Structural Biology
SN - 2059-7983
ER -
ID: 135365821