Molecular simulation of PcCel45A protein expressed from Aspergillus nidulans to understand its structure, dynamics, and thermostability

• Published in: Journal of molecular modeling Vol. 25; no. 11; pp. 317 - 7
• Main Authors: Unal, Mehmet Altay, Boyacioglu, Bahadir, Unver, Huseyin, Elmali, Ayhan
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.11.2019; Springer Nature B.V
• Subjects: Aspergillus nidulans - metabolism; beta-Glucosidase - metabolism; Biomass; Catalysis; Cellobiase; Cellulase - metabolism; Cellulose; Cellulose - metabolism; Characterization and Evaluation of Materials; Chemistry; Chemistry and Materials Science; Computer Appl. in Life Sciences; Computer Applications in Chemistry; Computer simulation; Dynamic stability; Endoglucanase; Fungal Proteins - metabolism; Glucosidase; Hydrolysis; Lignocellulose; Molecular dynamics; Molecular Dynamics Simulation; Molecular Medicine; Organic compounds; Original Paper; Proteins; Temperature; Temperature dependence; Theoretical and Computational Chemistry; Thermal stability; Molecular dynamics; PCcel45A
• ISSN: 1610-2940; 0948-5023; 0948-5023
• DOI: 10.1007/s00894-019-4175-4

PACS and mathematical subject classification numbers as needed. Molecular dynamic simulation is a very usable tool to understand various factors, including structure temperature dependence, dynamics, and stability for protein structure. The three main components, namely endoglucanase, exoglucanase, and β -glucosidase, effectively convert lignocellulosic biomass into fermentable sugar. Cellulose is the major component of plant cell walls and is the most abundant organic compound on the earth. Somewhat organisms can use cellulose as a food source, possessing cellulases (cellobiohydrolases and endoglucanases) that can catalyze the hydrolysis of the β -(1,4) glycosidic bonds. In this work, we investigated conformational and structural properties of PcCel45A protein by changing at temperatures with 300 K, 333 K, and 352 K. We found that the ASN92 residue was the major contributor to the stability of structure; some other residues correlated significantly with thermal stability. We also compared the theoretical results of the current study with the experimental ones published in previous studies.