1h57: Difference between revisions

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-[[Image:1h57.jpg|left|200px]]<br /><applet load="1h57" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1h57, resolution 1.60&Aring;" />
-'''STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND III'''<br />
-==Overview==
+==Structure of horseradish peroxidase C1A compound III==
-A molecular description of oxygen and peroxide activation in biological, systems is difficult, because electrons liberated during X-ray data, collection reduce the active centres of redox enzymes catalysing these, reactions. Here we describe an effective strategy to obtain crystal, structures for high-valency redox intermediates and present a, three-dimensional movie of the X-ray-driven catalytic reduction of a bound, dioxygen species in horseradish peroxidase (HRP). We also describe, separate experiments in which high-resolution structures could be obtained, for all five oxidation states of HRP, showing such structures with, preserved redox states for the first time.
+<StructureSection load='1h57' size='340' side='right'caption='[[1h57]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1h57]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H57 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H57 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]] 1.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</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=1h57 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h57 OCA], [https://pdbe.org/1h57 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h57 RCSB], [https://www.ebi.ac.uk/pdbsum/1h57 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h57 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PER1A_ARMRU PER1A_ARMRU] Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
+== 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/h5/1h57_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1h57 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-H57 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana] with <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=PEO:'>PEO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Peroxidase Peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7] Known structural/functional Site: <scene name='pdbsite=CAA:Peo+Binding+Site+For+Chain+A'>CAA</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H57 OCA].
+*[[Horseradish peroxidase|Horseradish peroxidase]]
+__TOC__
-==Reference==
+</StructureSection>
-The catalytic pathway of horseradish peroxidase at high resolution., Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J, Nature. 2002 May 23;417(6887):463-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12024218 12024218]
 [[Category: Armoracia rusticana]]
-[[Category: Peroxidase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Berglund GI]]
-[[Category: Berglund, G.I.]]
+[[Category: Carlsson GH]]
-[[Category: Carlsson, G.H.]]
+[[Category: Hajdu J]]
-[[Category: Hajdu, J.]]
-[[Category: Henriksen, A.]]
-[[Category: Smith, A.T.]]
-[[Category: Szoke, H.]]
-[[Category: ACT]]
-[[Category: CA]]
-[[Category: HEM]]
-[[Category: OXY]]
-[[Category: PEO]]
-[[Category: catalytic intermediate]]
-[[Category: compound iii]]
-[[Category: horseradish]]
-[[Category: oxidoreductase]]
-[[Category: oxyperoxidase]]
-[[Category: peroxidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:46:32 2008''