1izc | pdb_00001izc
Crystal Structure Analysis of Macrophomate synthase
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Overview
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.
About this Structure
1IZC is a Single protein structure of sequence from Macrophoma commelinae with MG and PYR as ligands. Full crystallographic information is available from OCA.
Reference
Insight into a natural Diels-Alder reaction from the structure of macrophomate synthase., Ose T, Watanabe K, Mie T, Honma M, Watanabe H, Yao M, Oikawa H, Tanaka I, Nature. 2003 Mar 13;422(6928):185-9. PMID:12634789
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