1tg5: Difference between revisions

Revision as of 00:06, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1tg5.png

Template:STRUCTURE 1tg5

Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645

Template:ABSTRACT PUBMED 15301540

About this StructureAbout this Structure

1TG5 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases., Yang C, Pflugrath JW, Camper DL, Foster ML, Pernich DJ, Walsh TA, Biochemistry. 2004 Aug 17;43(32):10414-23. PMID:15301540

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645'''
+===Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645===
-==Overview==
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-A high degree of selectivity toward the target site of the pest organism is a desirable attribute for new safer agrochemicals. To assist in the design of novel herbicides, we determined the crystal structures of the herbicidal target enzyme 4-hydroxyphenylpyruvate dioxygenase (HPPD; EC 1.13.11.27) from the plant Arabidopsis thaliana with and without an herbicidal benzoylpyrazole inhibitor that potently inhibits both plant and mammalian HPPDs. We also determined the structure of a mammalian (rat) HPPD in complex with the same nonselective inhibitor. From a screening campaign of over 1000 HPPD inhibitors, six highly plant-selective inhibitors were found. One of these had remarkable (&gt;1600-fold) selectivity toward the plant enzyme and was cocrystallized with Arabidopsis HPPD. Detailed comparisons of the plant and mammalian HPPD-ligand structures suggest a structural basis for the high degree of plant selectivity of certain HPPD inhibitors and point to design strategies to obtain potent and selective inhibitors of plant HPPD as agrochemical leads.
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