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5aa6

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Revision as of 04:47, 25 May 2023

Homohexameric Structure of the second Vanadate-Dependent Bromoperoxidase (AnII) from Ascophyllum nodosum

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Retrieved from "http://52.214.119.220/wiki/index.php/5aa6"

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 <StructureSection load='5aa6' size='340' side='right'caption='[[5aa6]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5aa6]] is a 6 chain structure with 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=5AA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AA6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5aa6]] is a 6 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=5AA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AA6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=VO4:VANADATE+ION'>VO4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bromide_peroxidase Bromide peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.18 1.11.1.18] </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=5aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa6 OCA], [https://pdbe.org/5aa6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5aa6 RCSB], [https://www.ebi.ac.uk/pdbsum/5aa6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa6 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5aa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5aa6 OCA], [http://pdbe.org/5aa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5aa6 RCSB], [http://www.ebi.ac.uk/pdbsum/5aa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5aa6 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/K7ZUA3_ASCNO K7ZUA3_ASCNO]
-The sequence of bromoperoxidase II from the brown alga Ascophyllum nodosum was determined from a full length cloned cDNA, obtained from a tandem mass spectrometry RT-PCR-approach. The clone encodes a protein composed of 641 amino-acids, which provides a mature 67.4 kDa-bromoperoxidase II-protein (620 amino-acids). Based on 43% sequence homology with the previously characterized bromoperoxidase I from A. nodosum, a tertiary structure was modeled for the bromoperoxidase II. The structural model was refined on the basis of results from gel filtration and vanadate-binding studies, showing that the bromoperoxidase II is a hexameric metalloprotein, which binds 0.5 equivalents of vanadate as cofactor per 67.4 kDa-subunit, for catalyzing oxidation of bromide by hydrogen peroxide in a bi-bi-ping-pong mechanism (k(cat) = 153 s(-1), 22 degrees C, pH 5.9). Bromide thereby is converted into a bromoelectrophile of reactivity similar to molecular bromine, based on competition kinetic data on phenol bromination and correlation analysis. Reactivity provided by the bromoperoxidase II mimics biosynthesis of methyl 4-bromopyrrole-2-carboxylate, a natural product isolated from the marine sponge Axinella tenuidigitata.
-Molecular cloning, structure, and reactivity of the second bromoperoxidase from Ascophyllum nodosum.,Wischang D, Radlow M, Schulz H, Vilter H, Viehweger L, Altmeyer MO, Kegler C, Herrmann J, Muller R, Gaillard F, Delage L, Leblanc C, Hartung J Bioorg Chem. 2012 Oct;44:25-34. doi: 10.1016/j.bioorg.2012.05.003. Epub 2012 Jun , 23. PMID:22884431<ref>PMID:22884431</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5aa6" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Haloperoxidase|Haloperoxidase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Ascophyllum nodosum]]
-[[Category: Bromide peroxidase]]
 [[Category: Large Structures]]
-[[Category: Czjzek, M]]
+[[Category: Czjzek M]]
-[[Category: Dabin, J]]
+[[Category: Dabin J]]
-[[Category: Delage, L]]
+[[Category: Delage L]]
-[[Category: Hartung, J]]
+[[Category: Hartung J]]
-[[Category: Jeudy, A]]
+[[Category: Jeudy A]]
-[[Category: Leblanc, C]]
+[[Category: Leblanc C]]
-[[Category: Radlow, M]]
+[[Category: Radlow M]]
-[[Category: Bromoperoxidase]]
-[[Category: Brown algae]]
-[[Category: Oxidoreductase]]
-[[Category: Vanadium-dependant halogenperoxidase]]

5aa6

From Proteopedia

Revision as of 04:47, 25 May 2023

Homohexameric Structure of the second Vanadate-Dependent Bromoperoxidase (AnII) from Ascophyllum nodosum

Structural highlights

Function

See Also

Contents

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