ArticlePloS one2015
Structural Insight of a Trimodular Halophilic Cellulase with a Family 46 Carbohydrate-Binding Module.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Characterization of a novel halophilic and thermostable multifunctional cellulase from Ebinur Salt Lake.Scientific reports · 2025Article
- Linker-mediated domain separation enhances cold adaptation in cellulases.Protein science : a publication of the Protein Society · 2025Article
- Large-scale analysis of the genome of the rare alkaline-halophilic Stachybotrys microspora reveals 46 cellulase genes.FEBS open bio · 2023Article
- Tunnel engineering to accelerate product release for better biomass-degrading abilities in lignocellulolytic enzymes.Biotechnology for biofuels · 2019Article
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Authors and funding
7 authors.
Funding
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Abstract
Cellulases are the key enzymes used in the biofuel industry. A typical cellulase contains a catalytic domain connected to a carbohydrate-binding module (CBM) through a flexible linker. Here we report the structure of an atypical trimodular cellulase which harbors a catalytic domain, a CBM46 domain and a rigid CBM_X domain between them. The catalytic domain shows the features of GH5 family, while the CBM46 domain has a sandwich-like structure. The catalytic domain and the CBM46 domain form an extended substrate binding cleft, within which several tryptophan residues are well exposed. Mutagenesis assays indicate that these residues are essential for the enzymatic activities. Gel affinity electrophoresis shows that these tryptophan residues are involved in the polysaccharide substrate binding. Also, electrostatic potential analysis indicates that almost the entire solvent accessible surface of CelB is negatively charged, which is consistent with the halophilic nature of this enzyme.
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