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| | == Structural highlights == | | == Structural highlights == |
| | <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> | | <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> |
| - | </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=VO4:VANADATE+ION'>VO4</scene></td></tr> | + | </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> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span></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=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> | | <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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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>
| + | [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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Ascophyllum nodosum]] | | [[Category: Ascophyllum nodosum]] |
| - | [[Category: Chloride peroxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hecht, H J]] | + | [[Category: Hecht H-J]] |
| - | [[Category: Kiess, M]] | + | [[Category: Kiess M]] |
| - | [[Category: Liaud, M F]] | + | [[Category: Liaud MF]] |
| - | [[Category: Schomburg, D]] | + | [[Category: Schomburg D]] |
| - | [[Category: Vilter, H]] | + | [[Category: Vilter H]] |
| - | [[Category: Weyand, M]] | + | [[Category: Weyand M]] |
| - | [[Category: Bromoperoxidase]]
| + | |
| - | [[Category: Haloperoxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Vanadium]]
| + | |
| Structural highlights
Function
PRXV_ASCNO Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D. X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution. J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953 doi:10.1006/jmbi.1999.3179
- ↑ Vilter H. Vanadium-dependent haloperoxidases. Met Ions Biol Syst. 1995;31:325-62. PMID:8564812
- ↑ Weyand M, Hecht H, Kiess M, Liaud M, Vilter H, Schomburg D. X-ray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nodosum at 2.0 A resolution. J Mol Biol. 1999 Oct 29;293(3):595-611. PMID:10543953 doi:10.1006/jmbi.1999.3179
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