1IZC
Crystal Structure Analysis of Macrophomate synthase
Summary for 1IZC
| Entry DOI | 10.2210/pdb1izc/pdb |
| Descriptor | macrophomate synthase intermolecular Diels-Alderase, MAGNESIUM ION, PYRUVIC ACID, ... (4 entities in total) |
| Functional Keywords | tim-barrel, pyruvate mg(ii) complex, lyase |
| Biological source | Macrophoma commelinae |
| Total number of polymer chains | 1 |
| Total formula weight | 36384.26 |
| Authors | Ose, T.,Watanabe, K.,Mie, T.,Honma, M.,Watanabe, H.,Yao, M.,Oikawa, H.,Tanaka, I. (deposition date: 2002-10-01, release date: 2003-04-01, Last modification date: 2023-11-15) |
| Primary citation | 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 Cited by 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: 12634789DOI: 10.1038/nature01454 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
