The Energy Landscape for the Interaction of the Family 1 Carbohydrate-Binding Module and the Cellulose Surface is Altered by Hydrolyzed Glycosidic Bonds

A multiscale simulation model is used to construct potential and free energy surfaces for the carbohydrate-binding module [CBM] from an industrially important cellulase, Trichoderma reesei cellobiohydrolase I, on the hydrophobic face of a coarse-grained cellulose Iβ polymorph. We predict from comput...

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Bibliographic Details
Published in:The journal of physical chemistry. B 2009-08, Vol.113 (31), p.10994-11002
Main Authors: Bu, Lintao, Beckham, Gregg T, Crowley, Michael F, Chang, Christopher H, Matthews, James F, Bomble, Yannick J, Adney, William S, Himmel, Michael E, Nimlos, Mark R
Format: Article
Language:English
Subjects:
09 BIOMASS FUELS
B: Biophysical Chemistry
BASIC BIOLOGICAL SCIENCES
Bioenergy
CELLOBIOSE
CELLULASE
CELLULOSE
Cellulose - chemistry
Cellulose - metabolism
Cellulose 1,4-beta-Cellobiosidase - chemistry
Cellulose 1,4-beta-Cellobiosidase - metabolism
CHAINS
Chemical and Biosciences
Computational Sciences
ENZYMES
FREE ENERGY
GLUCOSE
HYDROLYSIS
Hydrophobic and Hydrophilic Interactions
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
Materials Science and Semiconductors
Models, Molecular
Molecular Conformation
SIMULATION
STABILITY
THERMODYNAMICS
Trichoderma - enzymology
TRICHODERMA VIRIDE
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Summary:A multiscale simulation model is used to construct potential and free energy surfaces for the carbohydrate-binding module [CBM] from an industrially important cellulase, Trichoderma reesei cellobiohydrolase I, on the hydrophobic face of a coarse-grained cellulose Iβ polymorph. We predict from computation that the CBM alone exhibits regions of stability on the hydrophobic face of cellulose every 5 and 10 Å, corresponding to a glucose unit and a cellobiose unit, respectively. In addition, we predict a new role for the CBM: specifically, that in the presence of hydrolyzed cellulose chain ends, the CBM exerts a thermodynamic driving force to translate away from the free cellulose chain ends. This suggests that the CBM is not only required for binding to cellulose, as has been known for two decades, but also that it has evolved to both assist the enzyme in recognizing a cellulose chain end and exert a driving force on the enzyme during processive hydrolysis of cellulose.
ISSN:1520-6106
1520-5207
DOI:10.1021/jp904003z