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...

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Autores principales: Karkehabadi, Saeid, Hansson, Henrik, Mikkelsen, Nils Egil, Kim, Steve, Kaper, Thijs, Sandgren, Mats, Gudmundsson, Mikael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2018
Materias:
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.
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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
title_full Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
title_fullStr Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
title_full_unstemmed Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
title_short Structural studies of a glycoside hydrolase family 3 β-glucosidase from the model fungus Neurospora crassa
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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