𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

✍ Scribed by Osmair V. Oliveira; Luiz C. G. Freitas; T. P. Straatsma; Roberto D. Lins

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
429 KB
Volume
22
Category
Article
ISSN
0952-3499

No coin nor oath required. For personal study only.

✦ Synopsis

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.

📜 SIMILAR VOLUMES

Determination of the molecular states of
Determination of the molecular states of the processive endocellulase Thermobifida fusca Cel9A during crystalline cellulose depolymerization
✍ Maxim Kostylev; Jose M. Moran-Mirabal; Larry P. Walker; David B. Wilson 📂 Article 📅 2011 🏛 John Wiley and Sons 🌐 English ⚖ 178 KB

## Abstract Detailed understanding of cell wall degrading enzymes is important for their modeling and industrial applications, including in the production of biofuels. Here we used Cel9A, a processive endocellulase from __Thermobifida fusca,__ to demonstrate that cellulases that contain a catalytic