Impact of cellulose properties on enzymatic degradation by bacterial GH48 enzymes: Structural and mechanistic insights from processive Bacillus licheniformis Cel48B cellulase
| Autor: | Igor Polikarpov, Munir S. Skaf, Evandro Ares de Araújo, Vanessa de Oliveira Arnoldi Pellegrini, Luiz Pereira Ramos, Marco Antonio Seiki Kadowaki, Artur Hermano Sampaio Dias, Vasily Piyadov, Mateus Barbian Urio |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Models
Molecular Polymers and Plastics 02 engineering and technology Cellulase Molecular Dynamics Simulation Crystallography X-Ray 010402 general chemistry 01 natural sciences Substrate Specificity chemistry.chemical_compound Catalytic Domain Materials Chemistry Bacillus licheniformis Cellulases Cellulose chemistry.chemical_classification biology Hydrolysis Organic Chemistry Active site Substrate (chemistry) Processivity 021001 nanoscience & nanotechnology biology.organism_classification ENZIMAS 0104 chemical sciences Enzyme chemistry biology.protein Biophysics Statistical coupling analysis 0210 nano-technology Protein Binding |
| Zdroj: | Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual) Universidade de São Paulo (USP) instacron:USP |
| ISSN: | 0144-8617 |
| DOI: | 10.1016/j.carbpol.2021.118059 |
| Popis: | Processive cellulases are highly efficient molecular engines involved in the cellulose breakdown process. However, the mechanism that processive bacterial enzymes utilize to recruit and retain cellulose strands in the catalytic site remains poorly understood. Here, integrated enzymatic assays, protein crystallography and computational approaches were combined to study the enzymatic properties of the processive BlCel48B cellulase from Bacillus licheniformis. Hydrolytic efficiency, substrate binding affinity, cleavage patterns, and the apparent processivity of bacterial BlCel48B are significantly impacted by the cellulose size and its surface morphology. BlCel48B crystallographic structure was solved with ligands spanning -5 to -2 and +1 to +2 subsites. Statistical coupling analysis and molecular dynamics show that co-evolved residues on active site are critical for stabilizing ligands in the catalytic tunnel. Our results provide mechanistic insights into BlCel48B molecular-level determinants of activity, substrate binding, and processivity on insoluble cellulose, thus shedding light on structure-activity correlations of GH48 family members in general. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect