Interaction between the CBM of Cel9A from  Thermobifida fusca  and cellulose fibers | Zendy

Oliveira Osmair V. | Zendy; Freitas Luiz C. G. | Zendy; Straatsma T. P. | Zendy; Lins Roberto D. | Zendy

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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.

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