کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2049058 1074113 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Molecular simulations provide new insights into the role of the accessory immunoglobulin-like domain of Cel9A
چکیده انگلیسی

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 584, Issue 15, 4 August 2010, Pages 3431–3435
نویسندگان
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