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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...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2020
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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. |
format | Online Article Text |
id | pubmed-7604909 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
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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