1IZC

Crystal Structure Analysis of Macrophomate synthase

1IZC の概要

• エントリーDOI: 10.2210/pdb1izc/pdb
• 分子名称: macrophomate synthase intermolecular Diels-Alderase, MAGNESIUM ION, PYRUVIC ACID, ... (4 entities in total)
• 機能のキーワード: tim-barrel, pyruvate mg(ii) complex, lyase
• 由来する生物種: Macrophoma commelinae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36384.26

構造登録者

Ose, T.,Watanabe, K.,Mie, T.,Honma, M.,Watanabe, H.,Yao, M.,Oikawa, H.,Tanaka, I. (登録日: 2002-10-01, 公開日: 2003-04-01, 最終更新日: 2023-11-15)

主引用文献

Ose, T.,Watanabe, K.,Mie, T.,Honma, M.,Watanabe, H.,Yao, M.,Oikawa, H.,Tanaka, I.
Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase.
Nature, 422:185-189, 2003

PubMed Abstract: The Diels-Alder reaction, which forms a six-membered ring from an alkene (dienophile) and a 1,3-diene, is synthetically very useful for construction of cyclic products with high regio- and stereoselectivity under mild conditions. It has been applied to the synthesis of complex pharmaceutical and biologically active compounds. Although evidence on natural Diels-Alderases has been accumulated in the biosynthesis of secondary metabolites, there has been no report on the structural details of the natural Diels-Alderases. The function and catalytic mechanism of the natural Diels-Alderase are of great interest owing to the diversity of molecular skeletons in natural Diels-Alder adducts. Here we present the 1.70 A resolution crystal structure of the natural Diels-Alderase, fungal macrophomate synthase (MPS), in complex with pyruvate. The active site of the enzyme is large and hydrophobic, contributing amino acid residues that can hydrogen-bond to the substrate 2-pyrone. These data provide information on the catalytic mechanism of MPS, and suggest that the reaction proceeds via a large-scale structural reorganization of the product.

PubMed: 12634789
DOI: 10.1038/nature01454

実験手法

X-RAY DIFFRACTION (1.7 Å)