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Interaction between the CBM of Cel9A from Thermobifida fusca and cellulose fibers
Author(s) -
Oliveira Osmair V.,
Freitas Luiz C. G.,
Straatsma T. P.,
Lins Roberto D.
Publication year - 2008
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.925
Subject(s) - hydrogen bond , chemistry , amide , cellulose , amine gas treating , catalysis , molecular dynamics , docking (animal) , polysaccharide , carbohydrate binding module , stereochemistry , biochemistry , combinatorial chemistry , organic chemistry , cellulase , molecule , computational chemistry , medicine , nursing
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.