1idq

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[[Image:1idq.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF NATIVE VANADIUM-CONTAINING CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS==
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|PDB= 1idq |SIZE=350|CAPTION= <scene name='initialview01'>1idq</scene>, resolution 2.03&Aring;
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<StructureSection load='1idq' size='340' side='right'caption='[[1idq]], [[Resolution|resolution]] 2.03&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>
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<table><tr><td colspan='2'>[[1idq]] 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=1IDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IDQ 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]] 2.03&#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=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=1idq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1idq OCA], [https://pdbe.org/1idq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1idq RCSB], [https://www.ebi.ac.uk/pdbsum/1idq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1idq 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/id/1idq_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=1idq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Implications for the catalytic mechanism of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis have been obtained from the crystal structures of the native and peroxide forms of the enzyme.The X-ray structures have been solved by difference Fourier techniques using the atomic model of the azide chloroperoxidase complex. The 2.03 A crystal structure (R = 19.7%) of the native enzyme reveals the geometry of the intact catalytic vanadium center. The vanadium is coordinated by four non-protein oxygen atoms and one nitrogen (NE2) atom from histidine 496 in a trigonal bipyramidal fashion. Three oxygens are in the equatorial plane and the fourth oxygen and the nitrogen are at the apexes of the bipyramid. In the 2.24 A crystal structure (R = 17.7%) of the peroxide derivate the peroxide is bound to the vanadium in an eta2-fashion after the release of the apical oxygen ligand. The vanadium is coordinated also by 4 non-protein oxygen atoms and one nitrogen (NE2) from histidine 496. The coordination geometry around the vanadium is that of a distorted tetragonal pyramid with the two peroxide oxygens, one oxygen and the nitrogen in the basal plane and one oxygen in the apical position. A mechanism for the catalytic cycle has been proposed based on these X-ray structures and kinetic data.
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'''CRYSTAL STRUCTURE OF NATIVE VANADIUM-CONTAINING CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS'''
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Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form.,Messerschmidt A, Prade L, Wever R Biol Chem. 1997 Mar-Apr;378(3-4):309-15. PMID:9165086<ref>PMID:9165086</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1idq" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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Implications for the catalytic mechanism of the vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis have been obtained from the crystal structures of the native and peroxide forms of the enzyme.The X-ray structures have been solved by difference Fourier techniques using the atomic model of the azide chloroperoxidase complex. The 2.03 A crystal structure (R = 19.7%) of the native enzyme reveals the geometry of the intact catalytic vanadium center. The vanadium is coordinated by four non-protein oxygen atoms and one nitrogen (NE2) atom from histidine 496 in a trigonal bipyramidal fashion. Three oxygens are in the equatorial plane and the fourth oxygen and the nitrogen are at the apexes of the bipyramid. In the 2.24 A crystal structure (R = 17.7%) of the peroxide derivate the peroxide is bound to the vanadium in an eta2-fashion after the release of the apical oxygen ligand. The vanadium is coordinated also by 4 non-protein oxygen atoms and one nitrogen (NE2) from histidine 496. The coordination geometry around the vanadium is that of a distorted tetragonal pyramid with the two peroxide oxygens, one oxygen and the nitrogen in the basal plane and one oxygen in the apical position. A mechanism for the catalytic cycle has been proposed based on these X-ray structures and kinetic data.
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*[[Haloperoxidase|Haloperoxidase]]
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== References ==
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==About this Structure==
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<references/>
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1IDQ 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=1IDQ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Implications for the catalytic mechanism of the vanadium-containing enzyme chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures of the native and peroxide form., Messerschmidt A, Prade L, Wever R, Biol Chem. 1997 Mar-Apr;378(3-4):309-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9165086 9165086]
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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: Prade, L.]]
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[[Category: Prade L]]
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[[Category: Wever, R.]]
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[[Category: Wever R]]
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[[Category: VO4]]
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[[Category: two four-helix bundle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:48:59 2008''
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Current revision

CRYSTAL STRUCTURE OF NATIVE VANADIUM-CONTAINING CHLOROPEROXIDASE FROM CURVULARIA INAEQUALIS

PDB ID 1idq

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