1tg5: Difference between revisions

|PDB= 1tg5 |SIZE=350|CAPTION= <scene name='initialview01'>1tg5</scene>, resolution 1.9&Aring;

|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=645:[1-TERT-BUTYL-3-(2,4-DICHLOROPHENYL)-5-HYDROXY-1H-PYRAZOL-4-YL][2-CHLORO-4-(METHYLSULFONYL)PHENYL]METHANONE'>645</scene>

|ACTIVITY= [http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.11.27 1.3.11.27]  

|GENE= HPD, AT1G06570, F12K11.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])

'''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 (&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==

1TG5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TG5 OCA].

 

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:[http://www.ncbi.nlm.nih.gov/pubmed/15301540 15301540]

[[Category: Oxidoreductase]]

[[Category: Single protein]]

[[Category: Camper, D L.]]

[[Category: Foster, M L.]]

[[Category: Pernich, D J.]]

[[Category: Pflugrath, J W.]]

[[Category: Walsh, T A.]]

[[Category: Yang, C.]]

[[Category: hppd]]