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[[Image:1vnc.gif|left|200px]]


{{Structure
==CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS==
|PDB= 1vnc |SIZE=350|CAPTION= <scene name='initialview01'>1vnc</scene>, resolution 2.1&Aring;
<StructureSection load='1vnc' size='340' side='right'caption='[[1vnc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> and <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene>
<table><tr><td colspan='2'>[[1vnc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Curvularia_inaequalis Curvularia inaequalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VNC FirstGlance]. <br>
|ACTIVITY= [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]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</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=1vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vnc OCA], [https://pdbe.org/1vnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vnc RCSB], [https://www.ebi.ac.uk/pdbsum/1vnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vnc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRXC_CURIN PRXC_CURIN]
== 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/vn/1vnc_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=1vnc ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis belongs to a class of vanadium enzymes that oxidize halides in the presence of hydrogen peroxide to the corresponding hypohalous acids. The 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center. Azide coordinates directly to the metal center, resulting in a structure with azide, three nonprotein oxygens, and a histidine as ligands. In the native state vanadium will be bound as hydrogen vanadate(V) in a trigonal bipyramidal coordination with the metal coordinated to three oxygens in the equatorial plane, to the OH group at one apical position, and to the epsilon 2 nitrogen of a histidine at the other apical position. The protein fold is mainly alpha-helical with two four-helix bundles as main structural motifs and an overall structure different from other structures. The helices pack together to a compact molecule, which explains the high stability of the protein. An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine.


'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis.,Messerschmidt A, Wever R Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):392-6. PMID:8552646<ref>PMID:8552646</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1vnc" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis belongs to a class of vanadium enzymes that oxidize halides in the presence of hydrogen peroxide to the corresponding hypohalous acids. The 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center. Azide coordinates directly to the metal center, resulting in a structure with azide, three nonprotein oxygens, and a histidine as ligands. In the native state vanadium will be bound as hydrogen vanadate(V) in a trigonal bipyramidal coordination with the metal coordinated to three oxygens in the equatorial plane, to the OH group at one apical position, and to the epsilon 2 nitrogen of a histidine at the other apical position. The protein fold is mainly alpha-helical with two four-helix bundles as main structural motifs and an overall structure different from other structures. The helices pack together to a compact molecule, which explains the high stability of the protein. An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine.
*[[Haloperoxidase|Haloperoxidase]]
 
== References ==
==About this Structure==
<references/>
1VNC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Curvularia_inaequalis Curvularia inaequalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VNC OCA].
__TOC__
 
</StructureSection>
==Reference==
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis., Messerschmidt A, Wever R, Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):392-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8552646 8552646]
[[Category: Chloride peroxidase]]
[[Category: Curvularia inaequalis]]
[[Category: Curvularia inaequalis]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Messerschmidt, A.]]
[[Category: Messerschmidt A]]
[[Category: Wever, R.]]
[[Category: Wever R]]
[[Category: AZI]]
[[Category: VO4]]
[[Category: oxidoreductase]]
[[Category: vanadium-containing haloperoxidase]]
 
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Retrieved from "https://proteopedia.org/1vnc"