Interactions of the complete cellobiohydrolase I from Trichodera reesei with microcrystalline cellulose Iβ

• Published in: Cellulose (London) 2008-04, Vol.15 (2), p.261-273
• Main Authors: Zhong, Linghao, Matthews, James F, Crowley, Michael F, Rignall, Tauna, Talón, César, Cleary, Joseph M, Walker, Ross C, Chukkapalli, Giridhar, McCabe, Clare, Nimlos, Mark R, Brooks, Charles L. III, Himmel, Michael E, Brady, John W
• Format: Article
• Language: English
• Subjects: 09 BIOMASS FUELS; Aqueous environments; Bioorganic Chemistry; cellobiohydrolase I; Cellulase; Cellulose; Ceramics; Chemistry; Chemistry and Materials Science; Composites; computer modeling; Computer simulation; Crystalline cellulose; Domains; Fungi; Glass; Hypocrea jecorina; INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Molecular dynamics; Natural Materials; Oligosaccharides; Organic Chemistry; Physical Chemistry; Polymer Sciences; Spokes; Sustainable Development
• ISSN: 0969-0239; 1572-882X
• DOI: 10.1007/s10570-007-9186-0

We describe the construction of a model complex of the cellobiohydrolase I (CBH I) cellulase from Trichoderma reesei bound to a cellulose microfibril in an aqueous environment for use in molecular dynamics (MD) simulations. Preliminary characterization from the initial phases of an MD simulation of this complex is also described. The linker sequence between the two globular domains was found to be quite flexible, and the oligosaccharides bound to this linker were found to prefer to be splayed like the spokes in a wheel due to their hydration requirements. The overall conformations of the two globular domains remained stable in the simulations, although both underwent changes in their orientations.