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Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi

α-l-Arabinofuranosidases from glycoside hydrolase family 51 use a stereochemically retaining hydrolytic mechanism to liberate nonreducing terminal α-l-arabinofuranose residues from plant polysaccharides such as arabinoxylan and arabinan. To date, more than ten fungal GH51 α-l-arabinofuranosidases ha...

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Autores principales: McGregor, Nicholas G. S., Turkenburg, Johan P., Mørkeberg Krogh, Kristian B. R., Nielsen, Jens Erik, Artola, Marta, Stubbs, Keith A., Overkleeft, Herman S., Davies, Gideon J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7604909/
https://www.ncbi.nlm.nih.gov/pubmed/33135683
http://dx.doi.org/10.1107/S205979832001253X
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author McGregor, Nicholas G. S.
Turkenburg, Johan P.
Mørkeberg Krogh, Kristian B. R.
Nielsen, Jens Erik
Artola, Marta
Stubbs, Keith A.
Overkleeft, Herman S.
Davies, Gideon J.
author_facet McGregor, Nicholas G. S.
Turkenburg, Johan P.
Mørkeberg Krogh, Kristian B. R.
Nielsen, Jens Erik
Artola, Marta
Stubbs, Keith A.
Overkleeft, Herman S.
Davies, Gideon J.
author_sort McGregor, Nicholas G. S.
collection PubMed
description α-l-Arabinofuranosidases from glycoside hydrolase family 51 use a stereochemically retaining hydrolytic mechanism to liberate nonreducing terminal α-l-arabinofuranose residues from plant polysaccharides such as arabinoxylan and arabinan. To date, more than ten fungal GH51 α-l-arabinofuranosidases have been functionally characterized, yet no structure of a fungal GH51 enzyme has been solved. In contrast, seven bacterial GH51 enzyme structures, with low sequence similarity to the fungal GH51 enzymes, have been determined. Here, the crystallization and structural characterization of MgGH51, an industrially relevant GH51 α-l-arabinofuranosidase cloned from Meripilus giganteus, are reported. Three crystal forms were grown in different crystallization conditions. The unliganded structure was solved using sulfur SAD data collected from a single crystal using the I23 in vacuo diffraction beamline at Diamond Light Source. Crystal soaks with arabinose, 1,4-dideoxy-1,4-imino-l-arabinitol and two cyclophellitol-derived arabinose mimics reveal a conserved catalytic site and conformational itinerary between fungal and bacterial GH51 α-l-arabino­furanosidases.
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spelling pubmed-76049092020-11-17 Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi McGregor, Nicholas G. S. Turkenburg, Johan P. Mørkeberg Krogh, Kristian B. R. Nielsen, Jens Erik Artola, Marta Stubbs, Keith A. Overkleeft, Herman S. Davies, Gideon J. Acta Crystallogr D Struct Biol Research Papers α-l-Arabinofuranosidases from glycoside hydrolase family 51 use a stereochemically retaining hydrolytic mechanism to liberate nonreducing terminal α-l-arabinofuranose residues from plant polysaccharides such as arabinoxylan and arabinan. To date, more than ten fungal GH51 α-l-arabinofuranosidases have been functionally characterized, yet no structure of a fungal GH51 enzyme has been solved. In contrast, seven bacterial GH51 enzyme structures, with low sequence similarity to the fungal GH51 enzymes, have been determined. Here, the crystallization and structural characterization of MgGH51, an industrially relevant GH51 α-l-arabinofuranosidase cloned from Meripilus giganteus, are reported. Three crystal forms were grown in different crystallization conditions. The unliganded structure was solved using sulfur SAD data collected from a single crystal using the I23 in vacuo diffraction beamline at Diamond Light Source. Crystal soaks with arabinose, 1,4-dideoxy-1,4-imino-l-arabinitol and two cyclophellitol-derived arabinose mimics reveal a conserved catalytic site and conformational itinerary between fungal and bacterial GH51 α-l-arabino­furanosidases. International Union of Crystallography 2020-10-16 /pmc/articles/PMC7604909/ /pubmed/33135683 http://dx.doi.org/10.1107/S205979832001253X Text en © McGregor et al. 2020 http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/4.0/
spellingShingle Research Papers
McGregor, Nicholas G. S.
Turkenburg, Johan P.
Mørkeberg Krogh, Kristian B. R.
Nielsen, Jens Erik
Artola, Marta
Stubbs, Keith A.
Overkleeft, Herman S.
Davies, Gideon J.
Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title_full Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title_fullStr Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title_full_unstemmed Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title_short Structure of a GH51 α-l-arabinofuranosidase from Meripilus giganteus: conserved substrate recognition from bacteria to fungi
title_sort structure of a gh51 α-l-arabinofuranosidase from meripilus giganteus: conserved substrate recognition from bacteria to fungi
topic Research Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7604909/
https://www.ncbi.nlm.nih.gov/pubmed/33135683
http://dx.doi.org/10.1107/S205979832001253X
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