کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1941041 1050793 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A new approach to possible substrate binding mechanisms for nitrile hydratase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A new approach to possible substrate binding mechanisms for nitrile hydratase
چکیده انگلیسی

We combined normal mode analysis (NMA) with cavity calculations as a method to get more insight into static crystal structures. We used nitrile hydratase (NHase) as a case study, and the crystal structure of a complex of Pseudonocardia thermophila NHase (1UGP) with n-butyric acid was chosen as a reference structure. The reference structure was compared with the other available NHase crystal structures. Cavity calculations of the static structures showed the entrances to the active site and also a possible function of the N-terminal in the substrate selection of the Co-type NHase. When NMA was combined with cavity calculations, a closing–opening passage was observed. Analysis of low frequency modes combined with cavity calculations led us to propose “breathing” and “flip-flop” mechanisms which might be a key part of the substrate binding mechanism.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 343, Issue 1, 28 April 2006, Pages 319–325
نویسندگان
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