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[[Image:1h5j.jpg|left|200px]]
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{{STRUCTURE_1h5j|  PDB=1h5j  |  SCENE=  }}
'''X-RAY INDUCED REDUCTION OF HORSERADISH PEROXIDASE C1A COMPOUND III (67-78% DOSE)'''


==X-ray induced reduction of horseradish peroxidase C1A Compound III (67-78% dose)==
<StructureSection load='1h5j' size='340' side='right'caption='[[1h5j]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1h5j]] 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=1H5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5J 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=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=1h5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5j OCA], [https://pdbe.org/1h5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5j RCSB], [https://www.ebi.ac.uk/pdbsum/1h5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5j 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/h5/1h5j_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=1h5j ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:12024218</ref>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1H5J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5J OCA].
</div>
<div class="pdbe-citations 1h5j" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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://www.ncbi.nlm.nih.gov/pubmed/12024218 12024218]
*[[Horseradish peroxidase|Horseradish peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Armoracia rusticana]]
[[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: Henriksen, A.]]
[[Category: Smith AT]]
[[Category: Smith, A T.]]
[[Category: Szoke H]]
[[Category: Szoke, H.]]
[[Category: Compound iii]]
[[Category: Horseradish]]
[[Category: Oxidoreductase]]
[[Category: Oxyperoxidase]]
[[Category: Peroxidase]]
[[Category: X-ray induced reduction]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:27:34 2008''

Latest revision as of 07:24, 23 October 2024

X-ray induced reduction of horseradish peroxidase C1A Compound III (67-78% dose)

1h5j, resolution 1.60Å

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