ArticleBiophysical journal2013
Initial recognition of a cellodextrin chain in the cellulose-binding tunnel may affect cellobiohydrolase directional specificity.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 35 citations in OpenAlex.
- Molecular Details of Polyester Decrystallization via Molecular Simulation.Macromolecules · 2025Article
- Development of hybrid biomicroparticles: cellulose exposing functionalized fusion proteins.Microbial cell factories · 2024Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Efficient biomass saccharification using a novel cellobiohydrolase fromRSC advances · 2021Article
- Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
- Substrate binding in the processive cellulase Cel7A: Transition state of complexation and roles of conserved tryptophan residues.The Journal of biological chemistry · 2020Article
- Comparative insights into the saccharification potentials of a relatively unexplored but robustBiotechnology for biofuels · 2017Article
- Inter-domain Synergism Is Required for Efficient Feeding of Cellulose Chain into Active Site of Cellobiohydrolase Cel7A.The Journal of biological chemistry · 2016Article
- Kinetics of cellobiohydrolase (Cel7A) variants with lowered substrate affinity.The Journal of biological chemistry · 2014Article
- The tryptophan residue at the active site tunnel entrance of Trichoderma reesei cellobiohydrolase Cel7A is important for initiation of degradation of crystalline cellulose.The Journal of biological chemistry · 2013Article
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7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolases processively hydrolyze glycosidic linkages in individual polymer chains of cellulose microfibrils, and typically exhibit specificity for either the reducing or nonreducing end of cellulose. Here, we conduct molecular dynamics simulations and free energy calculations to examine the initial binding of a cellulose chain into the catalytic tunnel of the reducing-end-specific Family 7 cellobiohydrolase (Cel7A) from Hypocrea jecorina. In unrestrained simulations, the cellulose diffuses into the tunnel from the -7 to the -5 positions, and the associated free energy profiles exhibit no barriers for initial processivity. The comparison of the free energy profiles for different cellulose chain orientations show a thermodynamic preference for the reducing end, suggesting that the preferential initial binding may affect the directional specificity of the enzyme by impeding nonproductive (nonreducing end) binding. Finally, the Trp-40 at the tunnel entrance is shown with free energy calculations to have a significant effect on initial chain complexation in Cel7A.
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