Journal
JOURNAL OF MOLECULAR RECOGNITION
Volume 22, Issue 1, Pages 38-45Publisher
WILEY
DOI: 10.1002/jmr.925
Keywords
cellulase; CBM-cellulose interaction; molecular docking
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Funding
- CNPq
- FAPESP
- US Department of Energy (DOE) [DE-AC05-76RLO1830.]
- Department of Energy Office of Advanced Scientific Computing Research
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Molecular docking and molecular dynamics (MID) simulations were used to investigate the binding of a cellodextrin chain in a crystal-like conformation to the carbohydrate-binding module (CBM) of Cel9A from Thermobifida fusca. The fiber was found to bind to the CBM in a single and well-defined configuration in-line with the catalytic cleft, supporting the hypothesis that this CBM plays a role in the catalysis by feeding the catalytic domain (CD) with a polysaccharide chain. The results also expand the current known list of residues involved in the binding. The polysaccharide-protein attachment is shown to be mediated by five amine/amide-containing residues. E478 and E559 were found not to interact directly with the sugar chain; instead they seem to be responsible to stabilize the binding motif via hydrogen bonds. Copyright (C) 2008 John Wiley & Sons, Ltd.
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