1izc
From Proteopedia
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|PDB= 1izc |SIZE=350|CAPTION= <scene name='initialview01'>1izc</scene>, resolution 1.7Å | |PDB= 1izc |SIZE=350|CAPTION= <scene name='initialview01'>1izc</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1izc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1izc OCA], [http://www.ebi.ac.uk/pdbsum/1izc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1izc RCSB]</span> | ||
}} | }} | ||
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[[Category: Watanabe, K.]] | [[Category: Watanabe, K.]] | ||
[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: PYR]] | ||
[[Category: pyruvate mg(ii) complex]] | [[Category: pyruvate mg(ii) complex]] | ||
[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:26:48 2008'' |
Revision as of 18:26, 30 March 2008
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| , resolution 1.7Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analysis of Macrophomate synthase
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. 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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