ArticleThe Biochemical journal1999
Crystal structure of the catalytic core domain of the family 6 cellobiohydrolase II, Cel6A, from Humicola insolens, at 1.92 A resolution.
Article in The Biochemical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 74 citations in OpenAlex.
- Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.Chemical reviews · 2026Review
- Metagenomic mining and structure-function studies of a hyper-thermostable cellobiohydrolase from hot spring sediment.Communications biology · 2022Article
- Recombinant cellobiohydrolase of Myceliophthora thermophila: characterization and applicability in cellulose saccharification.AMB Express · 2021Article
- Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases.ACS omega · 2020Article
- The crystal structure of the chitinase ChiA74 of Bacillus thuringiensis has a multidomain assembly.Scientific reports · 2019Article
- 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
- Cellular automata modeling depicts degradation of cellulosic material by a cellulase system with single-molecule resolution.Biotechnology for biofuels · 2016Article
- The three-dimensional structure of the cellobiohydrolase Cel7A from Aspergillus fumigatus at 1.5 Å resolution.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Loop motions important to product expulsion in the Thermobifida fusca glycoside hydrolase family 6 cellobiohydrolase from structural and computational studies.The Journal of biological chemistry · 2013Article
- Gates of enzymes.Chemical reviews · 2013Review
- Insights into exo- and endoglucanase activities of family 6 glycoside hydrolases from Podospora anserina.Applied and environmental microbiology · 2013Article
- Two structurally discrete GH7-cellobiohydrolases compete for the same cellulosic substrate fiber.Biotechnology for biofuels · 2012Article
- Characterization of a cellobiohydrolase (MoCel6A) produced by Magnaporthe oryzae.Applied and environmental microbiology · 2010Article
- Processivity, synergism, and substrate specificity of Thermobifida fusca Cel6B.Applied and environmental microbiology · 2009Article
- Heterologous expression, crystallization and preliminary X-ray characterization of CcCel6C, a glycoside hydrolase family 6 enzyme from the basidiomycete Coprinopsis cinerea.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Protein disorder: conformational distribution of the flexible linker in a chimeric double cellulase.Biophysical journal · 2005Article
- A structural basis for processivity.Protein science : a publication of the Protein Society · 2001Review
- Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.The Biochemical journal · 2000Article
- Imaging the enzymatic digestion of bacterial cellulose ribbons reveals the endo character of the cellobiohydrolase Cel6A from Humicola insolens and its mode of synergy with cellobiohydrolase Cel7A.Applied and environmental microbiology · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
The three-dimensional structure of the catalytic core of the family 6 cellobiohydrolase II, Cel6A (CBH II), from Humicola insolens has been determined by X-ray crystallography at a resolution of 1.92 A. The structure was solved by molecular replacement using the homologous Trichoderma reesei CBH II as a search model. The H. insolens enzyme displays a high degree of structural similarity with its T. reesei equivalent. The structure features both O- (alpha-linked mannose) and N-linked glycosylation and a hexa-co-ordinate Mg2+ ion. The active-site residues are located within the enclosed tunnel that is typical for cellobiohydrolase enzymes and which may permit a processive hydrolysis of the cellulose substrate. The close structural similarity between the two enzymes implies that kinetics and chain-end specificity experiments performed on the H. insolens enzyme are likely to be applicable to the homologous T. reesei enzyme. These cast doubt on the description of cellobiohydrolases as exo-enzymes since they demonstrated that Cel6A (CBH II) shows no requirement for non-reducing chain-ends, as had been presumed. There is no crystallographic evidence in the present structure to support a mechanism involving loop opening, yet preliminary modelling experiments suggest that the active-site tunnel of Cel6A (CBH II) is too narrow to permit entry of a fluorescenyl-derivatized substrate, known to be a viable substrate for this enzyme.
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