ArticleThe Journal of biological chemistry2013
Loop motions important to product expulsion in the Thermobifida fusca glycoside hydrolase family 6 cellobiohydrolase from structural and computational studies.
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 17 papers.
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Who cites it
17 citing papers in PubMed, 41 citations in OpenAlex.
- There is an "I" in team: individual improvements in supercharged cellulase cocktail facilitates cooperative cellulose degradation.Biotechnology for biofuels and bioproducts · 2026Article
- Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.BBA advances · 2025Review
- Thermobifida fusca Cel6B moves bidirectionally while processively degrading cellulose.Biotechnology for biofuels and bioproducts · 2024Article
- The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A ofApplied and environmental microbiology · 2024Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Role for a Lytic Polysaccharide Monooxygenase in Cell Wall Remodeling in Streptomyces coelicolor.mBio · 2022Article
- Metagenomic mining and structure-function studies of a hyper-thermostable cellobiohydrolase from hot spring sediment.Communications biology · 2022Article
- A thermostable bacterial lytic polysaccharide monooxygenase with high operational stability in a wide temperature range.Biotechnology for biofuels · 2020Article
- Convergent evolution of processivity in bacterial and fungal cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- The hydrolysis mechanism of a GH45 cellulase and its potential relation to lytic transglycosylase and expansin function.The Journal of biological chemistry · 2020Article
- A mutation in an exoglucanase of Xanthomonas oryzae pv. oryzae, which confers an endo mode of activity, affects bacterial virulence, but not the induction of immune responses, in rice.Molecular plant pathology · 2018Article
- Advantages of a distant cellulase catalytic base.The Journal of biological chemistry · 2018Article
- Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose.The Journal of biological chemistry · 2016Article
- Cell wall targeted in planta iron accumulation enhances biomass conversion and seed iron concentration in Arabidopsis and rice.Plant biotechnology journal · 2016Article
- Evolution and Ecology of Actinobacteria and Their Bioenergy Applications.Annual review of microbiology · 2016Review
- Who's on base? Revealing the catalytic mechanism of inverting family 6 glycoside hydrolases.Chemical science · 2016Article
- Molecular origins of reduced activity and binding commitment of processive cellulases and associated carbohydrate-binding proteins to cellulose III.The Journal of biological chemistryArticle
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellobiohydrolases (CBHs) are typically major components of natural enzyme cocktails for biomass degradation. Their active sites are enclosed in a tunnel, enabling processive hydrolysis of cellulose chains. Glycoside hydrolase Family 6 (GH6) CBHs act from nonreducing ends by an inverting mechanism and are present in many cellulolytic fungi and bacteria. The bacterial Thermobifida fusca Cel6B (TfuCel6B) exhibits a longer and more enclosed active site tunnel than its fungal counterparts. Here, we determine the structures of two TfuCel6B mutants co-crystallized with cellobiose, D274A (catalytic acid), and the double mutant D226A/S232A, which targets the putative catalytic base and a conserved serine that binds the nucleophilic water. The ligand binding and the structure of the active site are retained when compared with the wild type structure, supporting the hypothesis that these residues are directly involved in catalysis. One structure exhibits crystallographic waters that enable construction of a model of the α-anomer product after hydrolysis. Interestingly, the product sites of TfuCel6B are completely enclosed by an "exit loop" not present in fungal GH6 CBHs and by an extended "bottom loop". From the structures, we hypothesize that either of the loops enclosing the product subsites in the TfuCel6B active site tunnel must open substantially for product release. With simulation, we demonstrate that both loops can readily open to allow product release with equal probability in solution or when the enzyme is engaged on cellulose. Overall, this study reveals new structural details of GH6 CBHs likely important for functional differences among enzymes from this important family.
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