1h58: Difference between revisions
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==STRUCTURE OF FERROUS HORSERADISH PEROXIDASE C1A== | ==STRUCTURE OF FERROUS HORSERADISH PEROXIDASE C1A== | ||
<StructureSection load='1h58' size='340' side='right' caption='[[1h58]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1h58' size='340' side='right' caption='[[1h58]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1atj|1atj]], [[1h55|1h55]], [[1h57|1h57]], [[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]], [[1h55|1h55]], [[1h57|1h57]], [[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=1h58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h58 OCA], [http://pdbe.org/1h58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h58 RCSB], [http://www.ebi.ac.uk/pdbsum/1h58 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=1h58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h58 OCA], [http://pdbe.org/1h58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h58 RCSB], [http://www.ebi.ac.uk/pdbsum/1h58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h58 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h58_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h58_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1h58" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1h58" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:53, 3 January 2018
STRUCTURE OF FERROUS HORSERADISH PEROXIDASE C1ASTRUCTURE OF FERROUS HORSERADISH PEROXIDASE C1A
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. References
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