We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2std

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2std.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2std.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2std| PDB=2std | SCENE= }}
{{STRUCTURE_2std| PDB=2std | SCENE= }}
-
'''SCYTALONE DEHYDRATASE COMPLEXED WITH TIGHT-BINDING INHIBITOR CARPROPAMID'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9665698}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9665698 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9665698}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Lyase]]
[[Category: Lyase]]
[[Category: Melanine biosynthesis]]
[[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 Sun Jul 27 13:38:08 2008''

Revision as of 10:38, 27 July 2008

Image:2std.png

Template:STRUCTURE 2std

SCYTALONE DEHYDRATASE COMPLEXED WITH TIGHT-BINDING INHIBITOR CARPROPAMID

Template:ABSTRACT PUBMED 9665698

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 Jul 27 13:38:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://proteopedia.org/wiki/index.php/2std"
Personal tools