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1qi9

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[[Image:1qi9.jpg|left|200px]]
 
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{{Structure
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==X-RAY SIRAS STRUCTURE DETERMINATION OF A VANADIUM-DEPENDENT HALOPEROXIDASE FROM ASCOPHYLLUM NODOSUM AT 2.0 A RESOLUTION==
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|PDB= 1qi9 |SIZE=350|CAPTION= <scene name='initialview01'>1qi9</scene>, resolution 2.05&Aring;
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<StructureSection load='1qi9' size='340' side='right'caption='[[1qi9]], [[Resolution|resolution]] 2.05&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=IOD:IODIDE ION'>IOD</scene>
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<table><tr><td colspan='2'>[[1qi9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascophyllum_nodosum Ascophyllum nodosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QI9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QI9 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene></td></tr>
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|GENE=
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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=1qi9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qi9 OCA], [https://pdbe.org/1qi9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qi9 RCSB], [https://www.ebi.ac.uk/pdbsum/1qi9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qi9 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PRXV_ASCNO PRXV_ASCNO] Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide.<ref>PMID:10543953</ref> <ref>PMID:8564812</ref>
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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/qi/1qi9_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=1qi9 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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The homo-dimeric structure of a vanadium-dependent haloperoxidase (V-BPO) from the brown alga Ascophyllum nodosum (EC 1.1.11.X) has been solved by single isomorphous replacement anomalous scattering (SIRAS) X-ray crystallography at 2.0 A resolution (PDB accession code 1QI9), using two heavy-atom datasets of a tungstate derivative measured at two different wavelengths. The protein sequence (SwissProt entry code P81701) of V-BPO was established by combining results from protein and DNA sequencing, and electron density interpretation. The enzyme has nearly an all-helical structure, with two four-helix bundles and only three small beta-sheets. The holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres. Structural similarity to the only other structurally characterized vanadium-dependent chloroperoxidase (V-CPO) from Curvularia inaequalis exists in the vicinity of the active site and to a lesser extent in the central four-helix bundle. Despite the low sequence and structural similarity between V-BPO and V-CPO, the vanadium binding centres are highly conserved on the N-terminal side of an alpha-helix and include the proposed catalytic histidine residue (His418(V-BPO)/His404(V-CPO)). The V-BPO structure contains, in addition, a second histidine near the active site (His411(V-BPO)), which can alter the redox potential of the catalytically active VO2-O2 species by protonation/deprotonation reactions. Specific binding sites for the organic substrates, like indoles and monochlordimedone, or for halide ions are not visible in the V-BPO structure. A reaction mechanism for the enzymatic oxidation of halides is discussed, based on the present structural, spectroscopic and biochemical knowledge of vanadium-dependent haloperoxidases, explaining the observed enzymatic differences between both enzymes.
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'''X-RAY SIRAS STRUCTURE DETERMINATION OF A VANADIUM-DEPENDENT HALOPEROXIDASE FROM ASCOPHYLLUM NODOSUM AT 2.0 A RESOLUTION'''
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X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution.,Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953<ref>PMID:10543953</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 1qi9" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The homo-dimeric structure of a vanadium-dependent haloperoxidase (V-BPO) from the brown alga Ascophyllum nodosum (EC 1.1.11.X) has been solved by single isomorphous replacement anomalous scattering (SIRAS) X-ray crystallography at 2.0 A resolution (PDB accession code 1QI9), using two heavy-atom datasets of a tungstate derivative measured at two different wavelengths. The protein sequence (SwissProt entry code P81701) of V-BPO was established by combining results from protein and DNA sequencing, and electron density interpretation. The enzyme has nearly an all-helical structure, with two four-helix bundles and only three small beta-sheets. The holoenzyme contains trigonal-bipyramidal coordinated vanadium atoms at its two active centres. Structural similarity to the only other structurally characterized vanadium-dependent chloroperoxidase (V-CPO) from Curvularia inaequalis exists in the vicinity of the active site and to a lesser extent in the central four-helix bundle. Despite the low sequence and structural similarity between V-BPO and V-CPO, the vanadium binding centres are highly conserved on the N-terminal side of an alpha-helix and include the proposed catalytic histidine residue (His418(V-BPO)/His404(V-CPO)). The V-BPO structure contains, in addition, a second histidine near the active site (His411(V-BPO)), which can alter the redox potential of the catalytically active VO2-O2 species by protonation/deprotonation reactions. Specific binding sites for the organic substrates, like indoles and monochlordimedone, or for halide ions are not visible in the V-BPO structure. A reaction mechanism for the enzymatic oxidation of halides is discussed, based on the present structural, spectroscopic and biochemical knowledge of vanadium-dependent haloperoxidases, explaining the observed enzymatic differences between both enzymes.
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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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1QI9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ascophyllum_nodosum Ascophyllum nodosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QI9 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution., Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D, J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10543953 10543953]
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[[Category: Ascophyllum nodosum]]
[[Category: Ascophyllum nodosum]]
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[[Category: Chloride peroxidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Hecht H-J]]
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[[Category: Hecht, H J.]]
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[[Category: Kiess M]]
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[[Category: Kiess, M.]]
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[[Category: Liaud MF]]
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[[Category: Liaud, M F.]]
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[[Category: Schomburg D]]
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[[Category: Schomburg, D.]]
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[[Category: Vilter H]]
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[[Category: Vilter, H.]]
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[[Category: Weyand M]]
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[[Category: Weyand, M.]]
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[[Category: IOD]]
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[[Category: VO4]]
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[[Category: bromoperoxidase]]
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[[Category: haloperoxidase]]
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[[Category: vanadium]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:55 2008''
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Current revision

X-RAY SIRAS STRUCTURE DETERMINATION OF A VANADIUM-DEPENDENT HALOPEROXIDASE FROM ASCOPHYLLUM NODOSUM AT 2.0 A RESOLUTION

PDB ID 1qi9

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