کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2052884 1074244 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition
چکیده انگلیسی

Here we report the first crystal structure of a protein, AmyA, a secretory α-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 Å resolution. AmyA lacks the conserved acidic surface, which is considered essential for protein stability at high salinity. Sedimentation velocity and CD experiments on AmyA reveal the formation of unique reversible poly-dispersed oligomers that show unusually high thermal stability. These studies provide valuable insight into the structural elements that contribute to the stability of AmyA at both physical and chemical extremes and their functional implications.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 580, Issue 11, 15 May 2006, Pages 2646–2652
نویسندگان
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