1tg5
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(New page: 200px<br /><applet load="1tg5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tg5, resolution 1.9Å" /> '''Crystal structures of...)
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Revision as of 01:07, 21 November 2007
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Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645
Overview
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 (>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.
About this Structure
1TG5 is a Single protein structure of sequence from Arabidopsis thaliana with FE2 and 645 as ligands. Active as Oxidoreductase, with EC number 1.3.11.27 Full crystallographic information is available from OCA.
Reference
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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