2w23

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{{Seed}}
 
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[[Image:2w23.png|left|200px]]
 
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==Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP)==
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The line below this paragraph, containing "STRUCTURE_2w23", creates the "Structure Box" on the page.
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<StructureSection load='2w23' size='340' side='right'caption='[[2w23]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2w23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2W23 FirstGlance]. <br>
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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]] 1.94&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2w23| PDB=2w23 | SCENE= }}
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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=2w23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2w23 OCA], [https://pdbe.org/2w23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2w23 RCSB], [https://www.ebi.ac.uk/pdbsum/2w23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2w23 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/VPL2_PLEER VPL2_PLEER] A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase.<ref>PMID:9987124</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/w2/2w23_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2w23 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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Lignin-degrading peroxidases, a group of biotechnologically-interesting enzymes,?oxidize high redox-potential aromatics via an exposed protein radical. Low-temperature EPR of Pleurotus eryngii versatile peroxidase (VP) revealed, for the first time in a fungal peroxidase, the presence of a tryptophanyl radical in both the two-electron (VPI) and one-electron (VPII) activated forms of the enzyme. Site-directed mutagenesis was used to substitute this tryptophan (Trp164) by tyrosine and histidine residues. No changes in the crystal structure were observed indicating that the modified behavior was due exclusively to the mutations introduced. EPR revealed the formation of tyrosyl radicals in both VPI and VPII of the W164Y variant. However, no protein radical was detected in the W164H variant, whose VPI spectrum indicated a porphyrin radical identical to that of the inactive W164S. Stopped-flow spectrophotometry showed that the W164Y mutation reduced 10-fold the apparent second-order rate constant for VPI reduction (k2app) by veratryl alcohol (VA), compared with over 50-fold reduction in W164S, revealing some catalytic activity of the tyrosine radical. Its first-order rate constant (k2) was more affected than the dissociation constant (KD2). Moreover, VPII reduction by VA was impaired by the above mutations revealing that the Trp164 radical was involved in catalysis by both VPI and VPII. The low first-order rate constant (k3) values were similar for the W164Y, W164H and W164S variants, indicating that the tyrosyl radical in VPII was not able to oxidize VA (in contrast with that observed for VPI). VPII self-reduction was also suppressed revealing that Trp164 is involved in this autocatalytic process.
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===STRUCTURE OF MUTANT W169Y OF PLEUROTUS ERYNGII VERSATILE PEROXIDASE (VP)===
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Protein radicals in fungal versatile peroxidase: Catalytic tryptophan radical in both Compound-I and Compound-II and studies on W164Y, W164H and W164S variants.,Ruiz-Duenas FJ, Pogni R, Morales M, Giansanti S, Mate MJ, Romero A, Martinez MJ, Basosi R, Martinez AT J Biol Chem. 2009 Jan 21. PMID:19158088<ref>PMID:19158088</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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The line below this paragraph, {{ABSTRACT_PUBMED_19158088}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2w23" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19158088 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19158088}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2W23 is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pleurotus_eryngii Pleurotus eryngii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2W23 OCA].
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==Reference==
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<ref group="xtra">PMID:19158088</ref><references group="xtra"/>
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[[Category: Pleurotus eryngii]]
[[Category: Pleurotus eryngii]]
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[[Category: Versatile peroxidase]]
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[[Category: Basosi R]]
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[[Category: Basosi, R.]]
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[[Category: Giansanti S]]
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[[Category: Giansanti, S.]]
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[[Category: Martinez AT]]
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[[Category: Martinez, A T.]]
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[[Category: Martinez MJ]]
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[[Category: Martinez, M J.]]
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[[Category: Mate MJ]]
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[[Category: Mate, M J.]]
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[[Category: Morales M]]
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[[Category: Morales, M.]]
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[[Category: Pogni R]]
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[[Category: Pogni, R.]]
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[[Category: Romero A]]
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[[Category: Romero, A.]]
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[[Category: Ruiz-Duenas FJ]]
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[[Category: Ruiz-Duenas, F J.]]
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[[Category: Calcium]]
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[[Category: Electron transfer]]
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[[Category: Glycoprotein]]
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[[Category: Heme]]
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[[Category: Hydrogen peroxide]]
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[[Category: Iron]]
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[[Category: Lignin degradation]]
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[[Category: Manganese]]
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[[Category: Manganese peroxidase]]
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[[Category: Metal-binding]]
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[[Category: Organic radical]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxidase]]
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[[Category: Protein radical]]
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[[Category: Secreted]]
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[[Category: Zymogen]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:38:58 2010''
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Current revision

Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP)

PDB ID 2w23

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