1std
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(New page: 200px<br /><applet load="1std" size="450" color="white" frame="true" align="right" spinBox="true" caption="1std, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 00:31, 21 November 2007
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CRYSTAL STRUCTURE OF SCYTALONE DEHYDRATASE: A DISEASE DETERMINANT OF THE RICE PATHOGEN, MAGNAPORTHE GRISEA
Overview
BACKGROUND: Rice blast is caused by the pathogenic fungus,-Magnaporthe, grisea. Non-pathogenic mutants have been identified that lack enzymes in, the biosynthetic pathway of dihydroxynapthalene-derived melanin. These, enzymes are therefore prime targets for fungicides designed to control, rice blast disease. One of the enzymes identified by genetic analysis as a, disease determinant is scytalone dehydratase. RESULTS: The, three-dimensional structure of scytalone dehydratase in complex with a, competitive inhibitor has been determined at 2.9 A resolution. A novel, fold, a cone-shaped alpha + beta barrel, is adopted by the monomer in this, trimeric protein, burying the hydrophobic active site in its interior. The, interactions of the inhibitor with the protein side chains have been, identified. The similarity of the inhibitor to the substrate and the side, chains involved in binding afford some insights into possible catalytic, mechanisms. CONCLUSIONS: These results provide a first look into the, structure and catalytic residues of a non-metal dehydratase, a large class, of hitherto structurally uncharacterized enzymes. It is envisaged that a, detailed structural description of scytalone dehydratase will assist in, the design of new inhibitors for controlling rice blast disease.
About this Structure
1STD is a Single protein structure of sequence from Magnaporthe grisea with SO4 and BFS as ligands. Active as Scytalone dehydratase, with EC number 4.2.1.94 Full crystallographic information is available from OCA.
Reference
Crystal structure of scytalone dehydratase--a disease determinant of the rice pathogen, Magnaporthe grisea., Lundqvist T, Rice J, Hodge CN, Basarab GS, Pierce J, Lindqvist Y, Structure. 1994 Oct 15;2(10):937-44. PMID:7866745
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