ArticleBiophysical journal2010
The O-glycosylated linker from the Trichoderma reesei Family 7 cellulase is a flexible, disordered protein.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 101 citations in OpenAlex.
- Deciphering How Clustered O‑Glycosylation Shapes Substrate-Binding Preferences in an Intrinsically Disordered Protein Region.JACS Au · 2026Article
- From the bench to the reactor: engineered filamentous fungi for biochemical and biomaterial production.Biotechnology for biofuels and bioproducts · 2025Review
- O-glycans Expand Lubricin and Attenuate Its Viscosity and Shear Thinning.Biomacromolecules · 2024Article
- TtCel7A: A Native Thermophilic Bifunctional Cellulose/Xylanase Exogluclanase from the Thermophilic Biomass-Degrading FungusJournal of fungi (Basel, Switzerland) · 2023Article
- A novel accessory protein ArCel5 from cellulose-gelatinizing fungus Arthrobotrys sp. CX1.Bioresources and bioprocessing · 2022Article
- The Linker Region Promotes Activity and Binding Efficiency of Modular LPMO towards Polymeric Substrate.Microbiology spectrum · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Article
- A linker of the proline-threonine repeating motif sequence is bimodal.Journal of molecular modeling · 2020Article
- Genomic and proteomic biases inform metabolic engineering strategies for anaerobic fungi.Metabolic engineering communications · 2020Article
- The impact ofChemical science · 2018Article
- Engineering enhanced cellobiohydrolase activity.Nature communications · 2018Article
- Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.Biotechnology for biofuels · 2018Article
- Correlation of structure, function and protein dynamics in GH7 cellobiohydrolases fromBiotechnology for biofuels · 2018Article
- Distinct roles of N- and O-glycans in cellulase activity and stability.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- A novel, highly efficient β-glucosidase with a cellulose-binding domain: characterization and properties of native and recombinant proteins.Biotechnology for biofuels · 2017Article
- Binding of cellulose binding modules reveal differences between cellulose substrates.Scientific reports · 2016Article
- Effect of Glycosylation on an Immunodominant Region in the V1V2 Variable Domain of the HIV-1 Envelope gp120 Protein.PLoS computational biology · 2016Article
- Effects of the linker region on the structure and function of modular GH5 cellulases.Scientific reports · 2016Article
- 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
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Authors and funding
16 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungi and bacteria secrete glycoprotein cocktails to deconstruct cellulose. Cellulose-degrading enzymes (cellulases) are often modular, with catalytic domains for cellulose hydrolysis and carbohydrate-binding modules connected by linkers rich in serine and threonine with O-glycosylation. Few studies have probed the role that the linker and O-glycans play in catalysis. Since different expression and growth conditions produce different glycosylation patterns that affect enzyme activity, the structure-function relationships that glycosylation imparts to linkers are relevant for understanding cellulase mechanisms. Here, the linker of the Trichoderma reesei Family 7 cellobiohydrolase (Cel7A) is examined by simulation. Our results suggest that the Cel7A linker is an intrinsically disordered protein with and without glycosylation. Contrary to the predominant view, the O-glycosylation does not change the stiffness of the linker, as measured by the relative fluctuations in the end-to-end distance; rather, it provides a 16 Å extension, thus expanding the operating range of Cel7A. We explain observations from previous biochemical experiments in the light of results obtained here, and compare the Cel7A linker with linkers from other cellulases with sequence-based tools to predict disorder. This preliminary screen indicates that linkers from Family 7 enzymes from other genera and other cellulases within T. reesei may not be as disordered, warranting further study.
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