Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A.

Abstract

Cel9A from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius belongs to the subfamily E1 of family 9 glycoside hydrolases, many members of which have an N-terminal Ig-like domain followed by the catalytic domain. The Ig-like domain is not directly involved in either carbohydrate binding or biocatalysis; however, deletion of the Ig-domain… (More)
DOI: 10.1016/j.febslet.2010.06.041

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@article{Liu2010MolecularSP, title={Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A.}, author={Hanbin Liu and Jos{\'e} Henrique Pereira and Paul D. Adams and Rajat Sapra and Blake A. Simmons and Kenneth L. Sale}, journal={FEBS letters}, year={2010}, volume={584 15}, pages={3431-5} }