Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
The glycoside hydrolase family 3 (GH3) β-glucosidases are a structurally diverse family of enzymes. Cel3A from Neurospora crassa (NcCel3A) belongs to a subfamily of key enzymes that are crucial for industrial biomass degradation. β-Glucosidases hydrolyse the β-1,4 bond at the nonreducing end of cell...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277957/ https://www.ncbi.nlm.nih.gov/pubmed/30511673 http://dx.doi.org/10.1107/S2053230X18015662 |
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author | Karkehabadi, Saeid Hansson, Henrik Mikkelsen, Nils Egil Kim, Steve Kaper, Thijs Sandgren, Mats Gudmundsson, Mikael |
author_facet | Karkehabadi, Saeid Hansson, Henrik Mikkelsen, Nils Egil Kim, Steve Kaper, Thijs Sandgren, Mats Gudmundsson, Mikael |
author_sort | Karkehabadi, Saeid |
collection | PubMed |
description | The glycoside hydrolase family 3 (GH3) β-glucosidases are a structurally diverse family of enzymes. Cel3A from Neurospora crassa (NcCel3A) belongs to a subfamily of key enzymes that are crucial for industrial biomass degradation. β-Glucosidases hydrolyse the β-1,4 bond at the nonreducing end of cellodextrins. The hydrolysis of cellobiose is of special importance as its accumulation inhibits other cellulases acting on crystalline cellulose. Here, the crystal structure of the biologically relevant dimeric form of NcCel3A is reported. The structure has been refined to 2.25 Å resolution, with an R (cryst) and R (free) of 0.18 and 0.22, respectively. NcCel3A is an extensively N-glycosylated glycoprotein that shares 46% sequence identity with Hypocrea jecorina Cel3A, the structure of which has recently been published, and 61% sequence identity with the thermophilic β-glucosidase from Rasamsonia emersonii. NcCel3A is a three-domain protein with a number of extended loops that deepen the active-site cleft of the enzyme. These structures characterize this subfamily of GH3 β-glucosidases and account for the high cellobiose specificity of this subfamily. |
format | Online Article Text |
id | pubmed-6277957 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-62779572018-12-13 Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa Karkehabadi, Saeid Hansson, Henrik Mikkelsen, Nils Egil Kim, Steve Kaper, Thijs Sandgren, Mats Gudmundsson, Mikael Acta Crystallogr F Struct Biol Commun Research Communications The glycoside hydrolase family 3 (GH3) β-glucosidases are a structurally diverse family of enzymes. Cel3A from Neurospora crassa (NcCel3A) belongs to a subfamily of key enzymes that are crucial for industrial biomass degradation. β-Glucosidases hydrolyse the β-1,4 bond at the nonreducing end of cellodextrins. The hydrolysis of cellobiose is of special importance as its accumulation inhibits other cellulases acting on crystalline cellulose. Here, the crystal structure of the biologically relevant dimeric form of NcCel3A is reported. The structure has been refined to 2.25 Å resolution, with an R (cryst) and R (free) of 0.18 and 0.22, respectively. NcCel3A is an extensively N-glycosylated glycoprotein that shares 46% sequence identity with Hypocrea jecorina Cel3A, the structure of which has recently been published, and 61% sequence identity with the thermophilic β-glucosidase from Rasamsonia emersonii. NcCel3A is a three-domain protein with a number of extended loops that deepen the active-site cleft of the enzyme. These structures characterize this subfamily of GH3 β-glucosidases and account for the high cellobiose specificity of this subfamily. International Union of Crystallography 2018-11-26 /pmc/articles/PMC6277957/ /pubmed/30511673 http://dx.doi.org/10.1107/S2053230X18015662 Text en © Karkehabadi et al. 2018 http://creativecommons.org/licenses/by/2.0/uk/ 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/2.0/uk/ |
spellingShingle | Research Communications Karkehabadi, Saeid Hansson, Henrik Mikkelsen, Nils Egil Kim, Steve Kaper, Thijs Sandgren, Mats Gudmundsson, Mikael Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa |
title | Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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title_full | Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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title_fullStr | Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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title_full_unstemmed | Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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title_short | Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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title_sort | structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus neurospora crassa |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6277957/ https://www.ncbi.nlm.nih.gov/pubmed/30511673 http://dx.doi.org/10.1107/S2053230X18015662 |
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