1tfz

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(New page: 200px<br /><applet load="1tfz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfz, resolution 1.8&Aring;" /> '''Structural basis for ...)
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caption="1tfz, resolution 1.8&Aring;" />
caption="1tfz, resolution 1.8&Aring;" />
'''Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases'''<br />
'''Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1TFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with FE and 869 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxyphenylpyruvate_dioxygenase 4-hydroxyphenylpyruvate dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.27 1.13.11.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TFZ OCA].
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1TFZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=869:'>869</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/4-hydroxyphenylpyruvate_dioxygenase 4-hydroxyphenylpyruvate dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.27 1.13.11.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFZ OCA].
==Reference==
==Reference==
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[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Camper, D.L.]]
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[[Category: Camper, D L.]]
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[[Category: Foster, M.L.]]
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[[Category: Foster, M L.]]
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[[Category: Pernich, D.J.]]
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[[Category: Pernich, D J.]]
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[[Category: Pflugrath, J.W.]]
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[[Category: Pflugrath, J W.]]
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[[Category: Walsh, T.A.]]
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[[Category: Walsh, T A.]]
[[Category: Yang, C.]]
[[Category: Yang, C.]]
[[Category: 869]]
[[Category: 869]]
[[Category: FE]]
[[Category: FE]]
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[[Category: 4-hydroxyphenylpyruvate dioxygenase]]
 
[[Category: arabidopsis thaliana]]
[[Category: arabidopsis thaliana]]
[[Category: athppd]]
[[Category: athppd]]
[[Category: hppd]]
[[Category: hppd]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:14:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:10 2008''

Revision as of 13:13, 21 February 2008


1tfz, resolution 1.8Å

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Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases

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

1TFZ is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Active as 4-hydroxyphenylpyruvate dioxygenase, with EC number 1.13.11.27 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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