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

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Standard

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.

In: Acta Crystallographica. Section D: Biological Crystallography, Vol. 71, 2015, p. 592-605.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Wong, MMJE, Midtgaard, SR, Gysel, K, Thygesen, MB, Sørensen, KK, Jensen, KJ, Stougaard, J, Thirup, SS & Blaise, M 2015, 'An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase', Acta Crystallographica. Section D: Biological Crystallography, vol. 71, pp. 592-605. https://doi.org/10.1107/S139900471402793X

APA

Wong, M. M. J. E., Midtgaard, S. R., Gysel, K., Thygesen, M. B., Sørensen, K. K., Jensen, K. J., ... Blaise, M. (2015). An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. Acta Crystallographica. Section D: Biological Crystallography, 71, 592-605. https://doi.org/10.1107/S139900471402793X

Vancouver

Wong MMJE, Midtgaard SR, Gysel K, Thygesen MB, Sørensen KK, Jensen KJ et al. An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. Acta Crystallographica. Section D: Biological Crystallography. 2015;71:592-605. https://doi.org/10.1107/S139900471402793X

Author

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. / An intermolecular binding mechanism involving multiple LysM domains mediates carbohydrate recognition by an endopeptidase. In: Acta Crystallographica. Section D: Biological Crystallography. 2015 ; Vol. 71. pp. 592-605.

Bibtex

@article{1c6001061a1146089e371b3e2b7a3785,
title = "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.",
author = "Wong, {Mei Mei Jaslyn Elizabeth} and Midtgaard, {S{\o}ren Roi} and Kira Gysel and Thygesen, {Mikkel Boas} and S{\o}rensen, {Kasper Kildegaard} and Jensen, {Knud J{\o}rgen} and Jens Stougaard and Thirup, {S{\o}ren Skou} and Mickael Blaise",
note = "OA",
year = "2015",
doi = "10.1107/S139900471402793X",
language = "English",
volume = "71",
pages = "592--605",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",

}

RIS

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