ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Substrate binding of a GH5 endoglucanase from the ruminal fungus Piromyces rhizinflata.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 29 citations in OpenAlex.
- Heterologous expression and biochemical characterization of a thermostable endo-β-1,4-glucanase from Colletotrichum orchidophilum.Bioprocess and biosystems engineering · 2021Article
- A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis.The Journal of biological chemistry · 2020Article
- Characterization of two GH5 endoglucanases from termite microbiome using synthetic metagenomics.Applied microbiology and biotechnology · 2020Article
- Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.Frontiers in bioengineering and biotechnology · 2020Review
- Activity and Thermostability of GH5 Endoglucanase Chimeras from Mesophilic and Thermophilic Parents.Applied and environmental microbiology · 2019Article
- Enhancing the catalytic activity of a novel GH5 cellulaseBiotechnology for biofuels · 2018Article
- Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism.Scientific reports · 2016Article
- Structure-Function Analysis of a Mixed-linkage β-Glucanase/Xyloglucanase from the Key Ruminal Bacteroidetes Prevotella bryantii B(1)4.The Journal of biological chemistry · 2016Article
- Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus.Scientific reports · 2015Article
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9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoglucanase EglA from Piromyces rhizinflata found in cattle stomach belongs to the GH5 family of glycoside hydrolases. The crystal structure of the catalytic domain of EglA shows the (β/α)(8)-barrel fold typical of GH5 enzymes. Adjacent to the active site of EglA, a loop containing a disulfide bond not found in other similar structures may participate in substrate binding. Because the active site was blocked by the N-terminal His tag of a neighbouring protein molecule in the crystal, enzyme-substrate complexes could not be obtained by soaking but were prepared by cocrystallization. The E154A mutant structure with a cellotriose bound to the -3, -2 and -1 subsites shows an extensive hydrogen-bonding network between the enzyme and the substrate, along with a stacking interaction between Trp44 and the -3 sugar. A possible dimer was observed in the crystal structure, but retention of activity in the E242A mutant suggested that the enzyme probably does not function as a dimer in solution. On the other hand, the first 100 amino acids encoded by the original cDNA fragment are very similar to those in the last third of the (β/α)(8)-barrel fold, indicating that EglA comprises at least two catalytic domains acting in tandem.
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