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2std
From Proteopedia
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[[Image:2std.gif|left|200px]] | [[Image:2std.gif|left|200px]] | ||
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'''SCYTALONE DEHYDRATASE COMPLEXED WITH TIGHT-BINDING INHIBITOR CARPROPAMID''' | '''SCYTALONE DEHYDRATASE COMPLEXED WITH TIGHT-BINDING INHIBITOR CARPROPAMID''' | ||
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[[Category: Nakasako, M.]] | [[Category: Nakasako, M.]] | ||
[[Category: Yamaguchi, I.]] | [[Category: Yamaguchi, I.]] | ||
| - | [[Category: | + | [[Category: Lyase]] |
| - | [[Category: | + | [[Category: Melanine biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:21:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 14:21, 4 May 2008
SCYTALONE DEHYDRATASE COMPLEXED WITH TIGHT-BINDING INHIBITOR CARPROPAMID
Overview
Scytalone dehydratase is a member of the group of enzymes involved in fungal melanin biosynthesis in a phytopathogenic fungus, Pyricularia oryzae, which causes rice blast disease. Carpropamid [(1RS,3SR)-2, 2-dichloro-N-[(R)-1-(4-chlorophenyl)ethyl]-1-ethyl-3-methylcyclopropa necarboxamide] is a tight-binding inhibitor of the enzyme. To clarify the structural basis for tight-binding inhibition, the crystal structure of the enzyme complexed with carpropamid was analyzed using diffraction data collected at 100 K. The structural model was refined to a crystallographic R-factor of 0.180 against reflections up to a resolution of 2.1 A. Carpropamid was bound in a hydrophobic cavity of the enzyme. Three types of interactions appeared to contribute to the binding. (i) A hydrogen bond was formed between a chloride atom in the dichloromethylethylcyclopropane ring of carpropamid and Asn-131 of the enzyme. (ii) The (chlorophenyl)ethyl group of carpropamid built strong contacts with Val-75, and this group further formed a cluster of aromatic rings together with four aromatic residues in the enzyme (Tyr-50, Phe-53, Phe-158, and Phe-162). (iii) Two hydration water molecules bound to the carboxamide group of carpropamid, and they were further hydrogen-bonded to Tyr-30, Tyr-50, His-85, and His-110. As a result of interactions between carpropamid and the phenylalanine residues (Phe-158 and Phe-162) in the C-terminal region of the enzyme, the C-terminal region completely covered the inhibitor, ensuring its localization in the cavity.
About this Structure
2STD is a Single protein structure of sequence from Magnaporthe grisea. Full crystallographic information is available from OCA.
Reference
Cryogenic X-ray crystal structure analysis for the complex of scytalone dehydratase of a rice blast fungus and its tight-binding inhibitor, carpropamid: the structural basis of tight-binding inhibition., Nakasako M, Motoyama T, Kurahashi Y, Yamaguchi I, Biochemistry. 1998 Jul 14;37(28):9931-9. PMID:9665698 Page seeded by OCA on Sun May 4 17:21:51 2008
