1tg5: Difference between revisions

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-{{STRUCTURE_1tg5|  PDB=1tg5  |  SCENE=  }}
-===Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645===
-{{ABSTRACT_PUBMED_15301540}}
-==About this Structure==
+==Crystal structures of plant 4-hydroxyphenylpyruvate dioxygenases complexed with DAS645==
-[[1tg5]] is a 1 chain structure with 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].
+<StructureSection load='1tg5' size='340' side='right'caption='[[1tg5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1tg5]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TG5 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg5 OCA], [https://pdbe.org/1tg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tg5 RCSB], [https://www.ebi.ac.uk/pdbsum/1tg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tg5 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HPPD_ARATH HPPD_ARATH]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tg/1tg5_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tg5 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
+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<ref>PMID:15301540</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1tg5" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Dioxygenase|Dioxygenase]]
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:015301540</ref><references group="xtra"/><references/>
+__TOC__
-[[Category: 4-hydroxyphenylpyruvate dioxygenase]]
+</StructureSection>
-[[Category: Arabidopsis thaliana]]
-[[Category: Camper, D L.]]
-[[Category: Foster, M L.]]
-[[Category: Pernich, D J.]]
-[[Category: Pflugrath, J W.]]
-[[Category: Walsh, T A.]]
-[[Category: Yang, C.]]
 [[Category: Arabidopsis thaliana]]
-[[Category: Athppd]]
+[[Category: Large Structures]]
-[[Category: Hppd]]
+[[Category: Camper DL]]
-[[Category: Oxidoreductase]]
+[[Category: Foster ML]]
+[[Category: Pernich DJ]]
+[[Category: Pflugrath JW]]
+[[Category: Walsh TA]]
+[[Category: Yang C]]