Joint X‐ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity

Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic enzymes, we report here the first crystal structure of the catalytic core domain of Cel7A (cellobiohydrolase I) from the filamentous fungus Trichoderma harzianum IOC 3844. Our structural studies and mol...

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Bibliographic Details
Published in:The FEBS journal 2013-01, Vol.280 (1), p.56-69
Main Authors: Textor, Larissa C., Colussi, Francieli, Silveira, Rodrigo L., Serpa, Viviane, Mello, Bruno L., Muniz, João Renato C., Squina, Fabio M., Pereira, Nei, Skaf, Munir S., Polikarpov, Igor
Format: Article
Language:English
Subjects:
Amino Acid Sequence
biomass
Biotechnology
Catalysis
Catalytic Domain
cellobiohydrolase
Cellulose
Cellulose 1,4-beta-Cellobiosidase - chemistry
Crystal structure
Crystallography, X-Ray
enzymatic hydrolysis
Hydrogen Bonding
Hypocrea jecorina
Kinetics
molecular dynamics
Molecular Dynamics Simulation
Molecular Sequence Data
Protein Structure, Secondary
Structural Homology, Protein
Trichoderma - enzymology
X‐ray structure
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Summary:Aiming to contribute toward the characterization of new, biotechnologically relevant cellulolytic enzymes, we report here the first crystal structure of the catalytic core domain of Cel7A (cellobiohydrolase I) from the filamentous fungus Trichoderma harzianum IOC 3844. Our structural studies and molecular dynamics simulations show that the flexibility of Tyr260, in comparison with Tyr247 from the homologous Trichoderma reesei Cel7A, is enhanced as a result of the short side‐chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. T. harzianum cellobiohydrolase I also has a shortened loop at the entrance of the cellulose‐binding tunnel, which has been described to interact with the substrate in T. reesei Cel7A. These structural features might explain why T. harzianum Cel7A displays higher kcat and Km values, and lower product inhibition on both glucoside and lactoside substrates, compared with T. reesei Cel7A. The crystal structure and molecular dynamics simulations the catalytic domain of exoglucanase Cel7A from T. harzianum are reported. The enzyme has a shortened loop at the entrance and more mobile loops that close up the cellulose‐binding tunnel. These features might explain why the enzyme displays higher kcat and Km values and lower product inhibition as compared to T. reesei Cel7A.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.12049