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1sp8

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(New page: 200px<br /><applet load="1sp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sp8, resolution 2.&Aring;" /> '''4-Hydroxyphenylpyruvat...)
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[[Image:1sp8.jpg|left|200px]]<br /><applet load="1sp8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1sp8, resolution 2.&Aring;" />
 
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'''4-Hydroxyphenylpyruvate Dioxygenase'''<br />
 
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==Overview==
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==4-Hydroxyphenylpyruvate Dioxygenase==
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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.
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<StructureSection load='1sp8' size='340' side='right'caption='[[1sp8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sp/1sp8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1SP8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with FE2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SP8 OCA].
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*[[Dioxygenase 3D structures|Dioxygenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=15084729 15084729]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Zea mays]]
[[Category: Zea mays]]
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[[Category: Auerbach, G.]]
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[[Category: Auerbach G]]
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[[Category: Freigang, J.]]
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[[Category: Freigang J]]
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[[Category: Fritze, I.M.]]
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[[Category: Fritze IM]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Linden, L.]]
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[[Category: Linden L]]
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[[Category: Steinbacher, S.]]
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[[Category: Steinbacher S]]
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[[Category: FE2]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:56:56 2007''
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Current revision

4-Hydroxyphenylpyruvate Dioxygenase

PDB ID 1sp8

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