ArticleActa crystallographica. Section F, Structural biology communications2017
Crystal structure of a family 6 cellobiohydrolase from the basidiomycete Phanerochaete chrysosporium.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part II. Structural Analysis of Thermotolerant Mutant from the BasidiomyceteJournal of applied glycoscience · 2024Article
- Thermotolerance Mechanism of Fungal GH6 Cellobiohydrolase. Part I. Characterization of Thermotolerant Mutant from the BasidiomyceteJournal of applied glycoscience · 2024Article
- Lytic polysaccharide monooxygenase increases cellobiohydrolases activity by promoting decrystallization of cellulose surface.Science advances · 2022Article
- Fluorescent Imaging of Extracellular Fungal Enzymes Bound onto Plant Cell Walls.International journal of molecular sciences · 2022Article
- Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases.The Journal of biological chemistry · 2020Article
- Thermostable Mutants of Glycoside Hydrolase Family 6 Cellobiohydrolase from the BasidiomyceteJournal of applied glycoscience · 2020Article
- The Secretome ofFrontiers in bioengineering and biotechnology · 2020Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cellobiohydrolases belonging to glycoside hydrolase family 6 (CBH II, Cel6A) play key roles in the hydrolysis of crystalline cellulose. CBH II from the white-rot fungus Phanerochaete chrysosporium (PcCel6A) consists of a catalytic domain (CD) and a carbohydrate-binding module connected by a linker peptide, like other known fungal cellobiohydrolases. In the present study, the CD of PcCel6A was crystallized without ligands, and p-nitrophenyl β-D-cellotrioside (pNPG3) was soaked into the crystals. The determined structures of the ligand-free and pNPG3-soaked crystals revealed that binding of cellobiose at substrate subsites +1 and +2 induces a conformational change of the N-terminal and C-terminal loops, switching the tunnel-shaped active site from the open to the closed form.
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