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==X- | |||
==X-ray induced reduction of horseradish peroxidase C1A Compound III (0-11% dose)== | |||
<StructureSection load='1h5d' size='340' side='right' caption='[[1h5d]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1h5d' size='340' side='right' caption='[[1h5d]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h5d]] is a 1 chain structure | <table><tr><td colspan='2'>[[1h5d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1atj|1atj]], [[1gw2|1gw2]], [[1gwo|1gwo]], [[1gwt|1gwt]], [[1gwu|1gwu]], [[1gx2|1gx2]], [[1h55|1h55]], [[1h57|1h57]], [[1h58|1h58]], [[1h5a|1h5a]], [[1h5c|1h5c]], [[1h5e|1h5e]], [[1h5f|1h5f]], [[1h5g|1h5g]], [[1h5h|1h5h]], [[1h5i|1h5i]], [[1h5j|1h5j]], [[1h5k|1h5k]], [[1h5l|1h5l]], [[1h5m|1h5m]], [[1hch|1hch]], [[2atj|2atj]], [[3atj|3atj]], [[6atj|6atj]], [[7atj|7atj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1atj|1atj]], [[1gw2|1gw2]], [[1gwo|1gwo]], [[1gwt|1gwt]], [[1gwu|1gwu]], [[1gx2|1gx2]], [[1h55|1h55]], [[1h57|1h57]], [[1h58|1h58]], [[1h5a|1h5a]], [[1h5c|1h5c]], [[1h5e|1h5e]], [[1h5f|1h5f]], [[1h5g|1h5g]], [[1h5h|1h5h]], [[1h5i|1h5i]], [[1h5j|1h5j]], [[1h5k|1h5k]], [[1h5l|1h5l]], [[1h5m|1h5m]], [[1hch|1hch]], [[2atj|2atj]], [[3atj|3atj]], [[6atj|6atj]], [[7atj|7atj]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5d OCA], [http://pdbe.org/1h5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5d RCSB], [http://www.ebi.ac.uk/pdbsum/1h5d PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5d OCA], [http://pdbe.org/1h5d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5d RCSB], [http://www.ebi.ac.uk/pdbsum/1h5d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1h5d ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Peroxidase]] | [[Category: Peroxidase]] | ||
[[Category: Berglund, G I]] | [[Category: Berglund, G I]] | ||
Revision as of 07:39, 21 September 2017
X-ray induced reduction of horseradish peroxidase C1A Compound III (0-11% dose)X-ray induced reduction of horseradish peroxidase C1A Compound III (0-11% dose)
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA 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. 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:12024218[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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