کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2828783 1162758 2011 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Crystal structure of a dimeric archaeal Cleavage and Polyadenylation Specificity Factor
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شناسی مولکولی
پیش نمایش صفحه اول مقاله
Crystal structure of a dimeric archaeal Cleavage and Polyadenylation Specificity Factor
چکیده انگلیسی

Proteins of the metallo-β-lactamase (MβL) fold form a large superfamily of metallo-hydrolase/oxidoreductases. Members of this family are found in all three domains of life and are involved in a variety of biological functions related to hydrolysis, redox processes, DNA repair and uptake, and RNA processing. We classified the archaeal homologs of this superfamily based on sequence similarity and characterized a subfamily of the Cleavage and Polyadenylation Specificity Factor (CPSF) with an uncommon domain composition: in addition to an extended MβL domain, which accommodates the active site for RNA cleavage, this group has two N-terminal KH domains. Here, we present the crystal structure of a member of this group from Methanosarcina mazei. It reveals a dimerization mode of the MβL domain that has not been observed before and suggests that RNA is bound across the dimer interface, recognized by the KH domains of one monomer, and cleaved at the active site of the other.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Structural Biology - Volume 173, Issue 1, January 2011, Pages 191–195
نویسندگان
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