Abstract
As part of our ongoing studies of thermophilic cellulases, we are examining the subfamily E1 of family 9 of glycoside hydrolases, members of which have an N-terminal immunoglobulin (Ig)-like domain followed by the catalytic domain (CD). While the function of the Ig-like module has not been determined, deletion of the Ig-domain results in complete loss of enzymatic activity in the cellobiohydrolase, CbhA from Clostridium thermocellum. In this work we used simulation approaches to investigate the role of the (Ig)-like domain in the non-processive endonuclease Cel9A from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius (Aa_Cel9A) for which the crystal structure has only recently been resolved.
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