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[[Image:2j5m.gif|left|200px]]<br />
<applet load="2j5m" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2j5m, resolution 1.75&Aring;" />
'''STRUCTURE OF CHLOROPEROXIDASE COMPOUND 0'''<br />


==Overview==
==Structure of Chloroperoxidase Compound 0==
We have determined the crystal structure of the chloroperoxidase (CPO), hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution., The intermediate was generated through controlled photoreduction of the, CPO oxygen complex during x-ray data collection, which was monitored by, recording of the crystal absorption spectra. Initially, the peroxo-anion, species was formed and then protonated to yield compound 0. Quantum, chemical calculations indicate that the peroxo-anion species is not stable, and collapses instantaneously to compound 0. Compound 0 is present in the, ferric low-spin doublet ground state and is characterized by a long O O, bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also, observed in the crystal structure.
<StructureSection load='2j5m' size='340' side='right'caption='[[2j5m]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2j5m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J5M 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]] 1.75&#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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=PRD_900111:2alpha-alpha-mannobiose'>PRD_900111</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=2j5m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5m OCA], [https://pdbe.org/2j5m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j5m RCSB], [https://www.ebi.ac.uk/pdbsum/2j5m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRXC_LEPFU PRXC_LEPFU] Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases.
== 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/j5/2j5m_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=2j5m ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound 0) at 1.75-A resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound 0. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound 0. Compound 0 is present in the ferric low-spin doublet ground state and is characterized by a long O O bond length of 1.5 A and a Fe O bond distance of 1.8 A, which is also observed in the crystal structure.


==About this Structure==
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes.,Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:17190816<ref>PMID:17190816</ref>
2J5M is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Leptoxyphium_fumago Leptoxyphium fumago]] with NAG, MAN, MN, ACT, HEM, PEO and EDO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J5M OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes., Kuhnel K, Derat E, Terner J, Shaik S, Schlichting I, Proc Natl Acad Sci U S A. 2007 Jan 2;104(1):99-104. Epub 2006 Dec 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17190816 17190816]
</div>
[[Category: Chloride peroxidase]]
<div class="pdbe-citations 2j5m" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Haloperoxidase|Haloperoxidase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leptoxyphium fumago]]
[[Category: Leptoxyphium fumago]]
[[Category: Single protein]]
[[Category: Derat E]]
[[Category: Derat, E.]]
[[Category: Kuhnel K]]
[[Category: Kuhnel, K.]]
[[Category: Schlichting I]]
[[Category: Schlichting, I.]]
[[Category: Shaik S]]
[[Category: Shaik, S.]]
[[Category: Terner J]]
[[Category: Terner, J.]]
[[Category: ACT]]
[[Category: EDO]]
[[Category: HEM]]
[[Category: MAN]]
[[Category: MN]]
[[Category: NAG]]
[[Category: PEO]]
[[Category: chloride]]
[[Category: glycoprotein]]
[[Category: heme]]
[[Category: iron]]
[[Category: manganese]]
[[Category: metal-binding]]
[[Category: oxidoreductase]]
[[Category: peroxidase]]
[[Category: pyrrolidone carboxylic acid]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:24:42 2007''
Retrieved from "https://proteopedia.org/2j5m"