Structural Basis for Herbicidal Inhibitor Selectivity Revealed by Comparison of Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases
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) f...
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Published in | Biochemistry (Easton) Vol. 43; no. 32; pp. 10414 - 10423 |
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Main Authors | , , , , , |
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Language | English |
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American Chemical Society
17.08.2004
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Abstract | 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. |
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AbstractList | 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. 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. |
Author | Yang, Cheng Walsh, Terence A Pflugrath, James W Camper, Debra L Pernich, Daniel J Foster, Mendy L |
Author_xml | – sequence: 1 givenname: Cheng surname: Yang fullname: Yang, Cheng – sequence: 2 givenname: James W surname: Pflugrath fullname: Pflugrath, James W – sequence: 3 givenname: Debra L surname: Camper fullname: Camper, Debra L – sequence: 4 givenname: Mendy L surname: Foster fullname: Foster, Mendy L – sequence: 5 givenname: Daniel J surname: Pernich fullname: Pernich, Daniel J – sequence: 6 givenname: Terence A surname: Walsh fullname: Walsh, Terence A |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15301540$$D View this record in MEDLINE/PubMed |
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Notes | Atomic coordinates of the HPPD complexes have been deposited in the Protein Data Bank (ID codes 1SQD, 1SQI, 1TFZ, 1TG5). istex:327A47DE11AEB5630F816BC8000CE0D8F2989B11 ark:/67375/TPS-DBW30GXN-8 |
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Snippet | 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... |
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SubjectTerms | 4-Hydroxyphenylpyruvate Dioxygenase - chemistry 4-Hydroxyphenylpyruvate Dioxygenase - metabolism Amino Acid Sequence Animals Arabidopsis - chemistry Arabidopsis - enzymology Arabidopsis - genetics Binding Sites Crystallography, X-Ray Enzyme Inhibitors - pharmacology Herbicides - pharmacology Models, Molecular Molecular Sequence Data Molecular Structure Protein Conformation Pyrazoles - pharmacology Rats Sequence Homology, Amino Acid Structure-Activity Relationship |
Title | Structural Basis for Herbicidal Inhibitor Selectivity Revealed by Comparison of Crystal Structures of Plant and Mammalian 4-Hydroxyphenylpyruvate Dioxygenases |
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