1std
From Proteopedia
(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 ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1std.gif|left|200px]]<br /><applet load="1std" size=" | + | [[Image:1std.gif|left|200px]]<br /><applet load="1std" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1std, resolution 2.9Å" /> | caption="1std, resolution 2.9Å" /> | ||
'''CRYSTAL STRUCTURE OF SCYTALONE DEHYDRATASE: A DISEASE DETERMINANT OF THE RICE PATHOGEN, MAGNAPORTHE GRISEA'''<br /> | '''CRYSTAL STRUCTURE OF SCYTALONE DEHYDRATASE: A DISEASE DETERMINANT OF THE RICE PATHOGEN, MAGNAPORTHE GRISEA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Rice blast is caused by the pathogenic fungus,-Magnaporthe | + | 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== | ==About this Structure== | ||
| - | 1STD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe grisea] with SO4 and BFS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Scytalone_dehydratase Scytalone dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.94 4.2.1.94] Full crystallographic information is available from [http:// | + | 1STD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Magnaporthe_grisea Magnaporthe grisea] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BFS:'>BFS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Scytalone_dehydratase Scytalone dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.94 4.2.1.94] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STD OCA]. |
==Reference== | ==Reference== | ||
| Line 20: | Line 20: | ||
[[Category: lyase (carbon-oxygen)]] | [[Category: lyase (carbon-oxygen)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:00 2008'' |
Revision as of 13:05, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 15:05:00 2008
