ArticleThe Journal of biological chemistry2013
Structural, biochemical, and computational characterization of the glycoside hydrolase family 7 cellobiohydrolase of the tree-killing fungus Heterobasidion irregulare.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 72 citations in OpenAlex.
- Genomic and Secretomic Analyses of the Newly Isolated FungusApplied and environmental microbiology · 2023Article
- Enzyme kinetics by GH7 cellobiohydrolases on chromogenic substrates is dictated by non-productive binding: insights from crystal structures and MD simulation.The FEBS journal · 2023Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Article
- Identification and Characterization of a Novel Hyperthermostable Bifunctional Cellobiohydrolase- Xylanase Enzyme for Synergistic Effect With Commercial Cellulase on Pretreated Wheat Straw Degradation.Frontiers in bioengineering and biotechnology · 2020Article
- Removal ofBiotechnology for biofuels · 2020Article
- The Secretome ofFrontiers in bioengineering and biotechnology · 2020Article
- A Conserved Glycoside Hydrolase Family 7 Cellobiohydrolase PsGH7a ofFrontiers in microbiology · 2020Article
- The dissociation mechanism of processive cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungusThe Journal of biological chemistry · 2019Article
- Engineering enhanced cellobiohydrolase activity.Nature communications · 2018Article
- Network of proteins, enzymes and genes linked to biomass degradation shared by Trichoderma species.Scientific reports · 2018Article
- Article
- Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases fromBiotechnology for biofuels · 2018Article
- Alanine substitution in cellobiohydrolase provides new insights into substrate threading.Scientific reports · 2017Article
- Improving the thermal stability of cellobiohydrolase Cel7A fromThe Journal of biological chemistry · 2017Article
- Comparative insights into the saccharification potentials of a relatively unexplored but robustBiotechnology for biofuels · 2017Article
- Biochemical and Structural Characterizations of Two Dictyostelium Cellobiohydrolases from the Amoebozoa Kingdom Reveal a High Level of Conservation between Distant Phylogenetic Trees of Life.Applied and environmental microbiology · 2016Article
- Comparing Residue Clusters from Thermophilic and Mesophilic Enzymes Reveals Adaptive Mechanisms.PloS one · 2016Article
- Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module.PloS one · 2015Article
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Root rot fungi of the Heterobasidion annosum complex are the most damaging pathogens in temperate forests, and the recently sequenced Heterobasidion irregulare genome revealed over 280 carbohydrate-active enzymes. Here, H. irregulare was grown on biomass, and the most abundant protein in the culture filtrate was identified as the only family 7 glycoside hydrolase in the genome, which consists of a single catalytic domain, lacking a linker and carbohydrate-binding module. The enzyme, HirCel7A, was characterized biochemically to determine the optimal conditions for activity. HirCel7A was crystallized and the structure, refined at 1.7 Å resolution, confirms that HirCel7A is a cellobiohydrolase rather than an endoglucanase, with a cellulose-binding tunnel that is more closed than Phanerochaete chrysosporium Cel7D and more open than Hypocrea jecorina Cel7A, suggesting intermediate enzyme properties. Molecular simulations were conducted to ascertain differences in enzyme-ligand interactions, ligand solvation, and loop flexibility between the family 7 glycoside hydrolase cellobiohydrolases from H. irregulare, H. jecorina, and P. chrysosporium. The structural comparisons and simulations suggest significant differences in enzyme-ligand interactions at the tunnel entrance in the -7 to -4 binding sites and suggest that a tyrosine residue at the tunnel entrance of HirCel7A may serve as an additional ligand-binding site. Additionally, the loops over the active site in H. jecorina Cel7A are more closed than loops in the other two enzymes, which has implications for the degree of processivity, endo-initiation, and substrate dissociation. Overall, this study highlights molecular level features important to understanding this biologically and industrially important family of glycoside hydrolases.
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