ArticleActa crystallographica. Section F, Structural biology communications2015
The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolution.
Article in Acta crystallographica. Section F, Structural biology communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 22 citations in OpenAlex.
- Powerful cell wall biomass degradation enzymatic system from saprotrophicCell surface (Amsterdam, Netherlands) · 2024Review
- The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A ofApplied and environmental microbiology · 2024Article
- Heterologous expression and characterization of glycoside hydrolase with its potential applications in hyperthermic environment.Saudi journal of biological sciences · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- A ThermostableInternational journal of molecular sciences · 2019Article
- Cellulases from Thermophiles Found by Metagenomics.Microorganisms · 2018Review
- Comparative insights into the saccharification potentials of a relatively unexplored but robustBiotechnology for biofuels · 2017Article
- Human Chitotriosidase Is an Endo-Processive Enzyme.PloS one · 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
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The enzymatic degradation of plant cell-wall cellulose is central to many industrial processes, including second-generation biofuel production. Key players in this deconstruction are the fungal cellobiohydrolases (CBHs), notably those from family GH7 of the carbohydrate-active enzymes (CAZY) database, which are generally known as CBHI enzymes. Here, three-dimensional structures are reported of the Aspergillus fumigatus CBHI Cel7A solved in uncomplexed and disaccharide-bound forms at resolutions of 1.8 and 1.5 Å, respectively. The product complex with a disaccharide in the +1 and +2 subsites adds to the growing three-dimensional insight into this family of industrially relevant biocatalysts.
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