1hch: Difference between revisions

New page: left|200px<br /> <applet load="1hch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hch, resolution 1.57Å" /> '''STRUCTURE OF HORSER...
 
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[[Image:1hch.gif|left|200px]]<br />
<applet load="1hch" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hch, resolution 1.57&Aring;" />
'''STRUCTURE OF HORSERADISH PEROXIDASE C1A COMPOUND I'''<br />


==Overview==
==Structure of horseradish peroxidase C1A compound I==
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='1hch' size='340' side='right'caption='[[1hch]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hch]] 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=1HCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCH 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]] 1.57&#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=O:OXYGEN+ATOM'>O</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=1hch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hch OCA], [https://pdbe.org/1hch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hch RCSB], [https://www.ebi.ac.uk/pdbsum/1hch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hch ProSAT]</span></td></tr>
</table>
== 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/hc/1hch_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=1hch 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.


==About this Structure==
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>
1HCH 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 ACT, CA, HEM and O as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HCH OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
<div class="pdbe-citations 1hch" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Horseradish peroxidase|Horseradish peroxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Armoracia rusticana]]
[[Category: Armoracia rusticana]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berglund, G.I.]]
[[Category: Berglund GI]]
[[Category: Carlsson, G.H.]]
[[Category: Carlsson GH]]
[[Category: Hajdu, J.]]
[[Category: Hajdu J]]
[[Category: Henriksen, A.]]
[[Category: Henriksen A]]
[[Category: Smith, A.T.]]
[[Category: Smith AT]]
[[Category: Szoke, H.]]
[[Category: Szoke H]]
[[Category: ACT]]
[[Category: CA]]
[[Category: HEM]]
[[Category: O]]
[[Category: catalytic intermediate]]
[[Category: compound i]]
[[Category: horseradish]]
[[Category: oxidoreductase]]
[[Category: peroxidase]]
 
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