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1vnc

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[[Image:1vnc.gif|left|200px]]
 
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{{Structure
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==CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS==
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|PDB= 1vnc |SIZE=350|CAPTION= <scene name='initialview01'>1vnc</scene>, resolution 2.1&Aring;
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<StructureSection load='1vnc' size='340' side='right'caption='[[1vnc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> and <scene name='pdbligand=AZI:AZIDE ION'>AZI</scene>
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<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>
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|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]
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</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>
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|GENE=
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<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>
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}}
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRXC_CURIN PRXC_CURIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vn/1vnc_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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'''CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS'''
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==See Also==
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*[[Haloperoxidase|Haloperoxidase]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Chloride peroxidase]]
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[[Category: Curvularia inaequalis]]
[[Category: Curvularia inaequalis]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Messerschmidt, A.]]
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[[Category: Messerschmidt A]]
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[[Category: Wever, R.]]
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[[Category: Wever R]]
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[[Category: AZI]]
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[[Category: VO4]]
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[[Category: oxidoreductase]]
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[[Category: vanadium-containing haloperoxidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:47:36 2008''
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Current revision

CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS

PDB ID 1vnc

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