1sp8: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1sp8.png|left|200px]]
-<!--
+==4-Hydroxyphenylpyruvate Dioxygenase==
-The line below this paragraph, containing "STRUCTURE_1sp8", creates the "Structure Box" on the page.
+<StructureSection load='1sp8' size='340' side='right'caption='[[1sp8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1sp8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SP8 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-{{STRUCTURE_1sp8|  PDB=1sp8  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1sp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sp8 OCA], [https://pdbe.org/1sp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sp8 RCSB], [https://www.ebi.ac.uk/pdbsum/1sp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sp8 ProSAT]</span></td></tr>
+</table>
+== 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/sp/1sp8_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=1sp8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The transformation of 4-hydroxyphenylpyruvate to homogentisate, catalyzed by 4-hydroxyphenylpyruvate dioxygenase (HPPD), plays an important role in degrading aromatic amino acids. As the reaction product homogentisate serves as aromatic precursor for prenylquinone synthesis in plants, the enzyme is an interesting target for herbicides. In this study we report the first x-ray structures of the plant HPPDs of Zea mays and Arabidopsis in their substrate-free form at 2.0 A and 3.0 A resolution, respectively. Previous biochemical characterizations have demonstrated that eukaryotic enzymes behave as homodimers in contrast to prokaryotic HPPDs, which are homotetramers. Plant and bacterial enzymes share the overall fold but use orthogonal surfaces for oligomerization. In addition, comparison of both structures provides direct evidence that the C-terminal helix gates substrate access to the active site around a nonheme ferrous iron center. In the Z. mays HPPD structure this helix packs into the active site, sequestering it completely from the solvent. In contrast, in the Arabidopsis structure this helix tilted by about 60 degrees into the solvent and leaves the active site fully accessible. By elucidating the structure of plant HPPD enzymes we aim to provide a structural basis for the development of new herbicides.
-===4-Hydroxyphenylpyruvate Dioxygenase===
+The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase.,Fritze IM, Linden L, Freigang J, Auerbach G, Huber R, Steinbacher S Plant Physiol. 2004 Apr;134(4):1388-400. PMID:15084729<ref>PMID:15084729</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1sp8" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_15084729}}, adds the Publication Abstract to the page
+*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 15084729 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15084729}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SP8 OCA].
+[[Category: Zea mays]]
+[[Category: Auerbach G]]
-==Reference==
+[[Category: Freigang J]]
-The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase., Fritze IM, Linden L, Freigang J, Auerbach G, Huber R, Steinbacher S, Plant Physiol. 2004 Apr;134(4):1388-400. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15084729 15084729]
+[[Category: Fritze IM]]
-[[Category: Auerbach, G.]]
+[[Category: Huber R]]
-[[Category: Freigang, J.]]
+[[Category: Linden L]]
-[[Category: Fritze, I M.]]
+[[Category: Steinbacher S]]
-[[Category: Huber, R.]]
-[[Category: Linden, L.]]
-[[Category: Steinbacher, S.]]
-[[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:02:20 2008''