3C2R

Crystal structure of the quinolinate phosphoribosyl transferase (BNA6) from Sachharomyces cerevisiae complexed with the inhibitor phthalate

3C2R の概要

• エントリーDOI: 10.2210/pdb3c2r/pdb
• 関連するPDBエントリー: 3C2D 3C2E 3C2F 3C2O 3C2V
• 分子名称: Nicotinate-nucleotide pyrophosphorylase, PHTHALIC ACID (3 entities in total)
• 機能のキーワード: qprtase, prtase, bna6, quinolinate, phthalate, cytoplasm, glycosyltransferase, nucleus, pyridine nucleotide biosynthesis, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Cytoplasm: P43619
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65136.09

構造登録者

di Luccio, E.,Wilson, D.K. (登録日: 2008-01-25, 公開日: 2008-04-01, 最終更新日: 2024-02-21)

主引用文献

di Luccio, E.,Wilson, D.K.
Comprehensive X-ray Structural Studies of the Quinolinate Phosphoribosyl Transferase (BNA6) from Saccharomyces cerevisiae.
Biochemistry, 47:4039-4050, 2008

PubMed Abstract: Quinolinic acid phosphoribosyl transferase (QAPRTase, EC 2.4.2.19) is a 32 kDa enzyme encoded by the BNA6 gene in yeast and catalyzes the formation of nicotinate mononucleotide from quinolinate and 5-phosphoribosyl-1-pyrophosphate (PRPP). QAPRTase plays a key role in the tryptophan degradation pathway via kynurenine, leading to the de novo biosynthesis of NAD (+) and clearing the neurotoxin quinolinate. To improve our understanding of the specificity of the eukaryotic enzyme and the course of events associated with catalysis, we have determined the crystal structures of the apo and singly bound forms with the substrates quinolinate and PRPP. This reveals that the enzyme folds in a manner similar to that of various prokaryotic forms which are approximately 30% identical in sequence. In addition, the structure of the Michaelis complex is approximated by PRPP and the quinolinate analogue phthalate bound to the active site. These results allow insight into the kinetic mechanism of QAPRTase and provide an understanding of structural diversity in the active site of the Saccharomyces cerevisiae enzyme when compared to prokaryotic homologues.

PubMed: 18321072
DOI: 10.1021/bi7020475

実験手法

X-RAY DIFFRACTION (2.4 Å)