کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8294027 | 1536750 | 2018 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The C2â²- and C3â²-endo equilibrium for AMP molecules bound in the cystathionine-beta-synthase domain
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: The C2â²- and C3â²-endo equilibrium for AMP molecules bound in the cystathionine-beta-synthase domain The C2â²- and C3â²-endo equilibrium for AMP molecules bound in the cystathionine-beta-synthase domain](/preview/png/8294027.png)
چکیده انگلیسی
The equilibrium between C2â²- and C3â²-endo conformations of nucleotides in solution, as well as their polymers DNA and RNA, has been well studied in previous work. However, this equilibrium of nucleotides in their binding state remains unclear. We observed two AMP molecules, in C3â²- and C2â²-endo conformations respectively, simultaneously bound to a cystathionine-beta-synthase (CBS) domain dimer of the magnesium and cobalt efflux protein CorC in the crystallographic study. The C2â²-endo AMP molecule assumes the higher sugar pucker energy and one more hydrogen bond with the protein than the C3â²-endo molecule does. The balance between the high sugar pucker energy and the low binding energy suggests an equilibrium or switch between C2â²- and C3â²-endo conformations of the bound nucleotides. Our work challenge the previous hypothesis that the ribose of the bound nucleotides would be locked in a fixed conformation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 497, Issue 2, 4 March 2018, Pages 646-651
Journal: Biochemical and Biophysical Research Communications - Volume 497, Issue 2, 4 March 2018, Pages 646-651
نویسندگان
Na Feng, Chao Qi, Yan-Jie Hou, Ying Zhang, Da-Cheng Wang, De-Feng Li,