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Molecular simulations provide new insights into the role of the accessory immunoglobulin‐like domain of Cel9A
Author(s) -
Liu Hanbin,
Pereira Jose Henrique,
Adams Paul D.,
Sapra Rajat,
Simmons Blake A.,
Sale Kenneth L.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.06.041
Subject(s) - antibody , domain (mathematical analysis) , immunoglobulin domain , computational biology , chemistry , immunoglobulin g , biology , immunology , mathematics , mathematical analysis
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 promotes loss of enzymatic activity. We have investigated the functional role of the Ig‐like domain using molecular dynamics simulations. Our simulations indicate that residues within the Ig‐like domain are dynamically correlated with residues in the carbohydrate‐binding pocket and with key catalytic residues of Cel9A. Free energy perturbation simulations indicate that the Ig‐like domain stabilizes the catalytic domain and may be responsible for the enhanced thermostability of Cel9A.