کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2187764 1096138 2008 16 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
The Crystal Structure of β-Alanine Synthase from Drosophila melanogaster Reveals a Homooctameric Helical Turn-Like Assembly
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
The Crystal Structure of β-Alanine Synthase from Drosophila melanogaster Reveals a Homooctameric Helical Turn-Like Assembly
چکیده انگلیسی

β-Alanine synthase (βAS) is the third enzyme in the reductive pyrimidine catabolic pathway, which is responsible for the breakdown of the nucleotide bases uracil and thymine in higher organisms. It catalyzes the hydrolysis of N-carbamyl-β-alanine and N-carbamyl-β-aminoisobutyrate to the corresponding β-amino acids. βASs are grouped into two phylogenetically unrelated subfamilies, a general eukaryote one and a fungal one. To reveal the molecular architecture and understand the catalytic mechanism of the general eukaryote βAS subfamily, we determined the crystal structure of Drosophila melanogaster βAS to 2.8 Å resolution. It shows a homooctameric assembly of the enzyme in the shape of a left-handed helical turn, in which tightly packed dimeric units are related by 2-fold symmetry. Such an assembly would allow formation of higher oligomers by attachment of additional dimers on both ends. The subunit has a nitrilase-like fold and consists of a central β-sandwich with a layer of α-helices packed against both sides. However, the core fold of the nitrilase superfamily enzymes is extended in D. melanogaster βAS by addition of several secondary structure elements at the N-terminus. The active site can be accessed from the solvent by a narrow channel and contains the triad of catalytic residues (Cys, Glu, and Lys) conserved in nitrilase-like enzymes.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 377, Issue 5, 11 April 2008, Pages 1544–1559
نویسندگان
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