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- Title
Interaction between the CBM of Cel9A from Thermobifida fusca and cellulose fibers.
- Authors
Oliveira, Osmair V.; Freitas, Luiz C. G.; Straatsma, T. P.; Lins, Roberto D.
- Abstract
Molecular docking and molecular dynamics (MD) 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 © 2008 John Wiley & Sons, Ltd.
- Publication
Journal of Molecular Recognition, 2009, Vol 22, Issue 1, p38
- ISSN
0952-3499
- Publication type
Article
- DOI
10.1002/jmr.925