1h5h

From Proteopedia

(Difference between revisions)

Current revision

X-ray induced reduction of horseradish peroxidase C1A Compound III (44-56% dose)

Structural highlights

1h5h is a 1 chain structure with sequence from Armoracia rusticana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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.

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

↑ Berglund GI, Carlsson GH, Smith AT, Szoke H, Henriksen A, Hajdu J. The catalytic pathway of horseradish peroxidase at high resolution. Nature. 2002 May 23;417(6887):463-8. PMID:12024218 doi:10.1038/417463a

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h5h"

@@ Line 3: / Line 3: @@
 <StructureSection load='1h5h' size='340' side='right'caption='[[1h5h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1h5h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Armru Armru]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1H5H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1h5h]] 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=1H5H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5H 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>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene></td></tr>
+</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='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]], [[1h5d|1h5d]], [[1h5e|1h5e]], [[1h5f|1h5f]], [[1h5g|1h5g]], [[1h5i|1h5i]], [[1h5j|1h5j]], [[1h5k|1h5k]], [[1h5l|1h5l]], [[1h5m|1h5m]], [[1hch|1hch]], [[2atj|2atj]], [[3atj|3atj]], [[6atj|6atj]], [[7atj|7atj]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=1h5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5h OCA], [https://pdbe.org/1h5h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5h RCSB], [https://www.ebi.ac.uk/pdbsum/1h5h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5h ProSAT]</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=1h5h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5h OCA], [http://pdbe.org/1h5h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h5h RCSB], [http://www.ebi.ac.uk/pdbsum/1h5h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5h ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 16: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h5/1h5h_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Armru]]
+[[Category: Armoracia rusticana]]
 [[Category: Large Structures]]
-[[Category: Peroxidase]]
+[[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: X-ray induced reduction]]

1h5h

From Proteopedia

Current revision

X-ray induced reduction of horseradish peroxidase C1A Compound III (44-56% dose)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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