4g2c

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==DyP2 from Amycolatopsis sp. ATCC 39116==
==DyP2 from Amycolatopsis sp. ATCC 39116==
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<StructureSection load='4g2c' size='340' side='right' caption='[[4g2c]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='4g2c' size='340' side='right'caption='[[4g2c]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4g2c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Amycolatopsis_sp._atcc_39116 Amycolatopsis sp. atcc 39116]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G2C FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4g2c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Amycolatopsis_sp._ATCC_39116 Amycolatopsis sp. ATCC 39116]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G2C FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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]] 2.25&#8491;</td></tr>
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<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=4g2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4g2c RCSB], [http://www.ebi.ac.uk/pdbsum/4g2c PDBsum]</span></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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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=4g2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g2c OCA], [https://pdbe.org/4g2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g2c RCSB], [https://www.ebi.ac.uk/pdbsum/4g2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g2c ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DYP2_AMYS7 DYP2_AMYS7]
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Plant biomass represents a renewable feedstock that has not yet been fully tapped because of the difficulty in accessing the carbon in its structural biopolymers. Lignin is an especially challenging substrate, but select microbes have evolved complex systems of enzymes for its breakdown through a radical-mediated oxidation process. Fungal systems are well-characterized for their ability to depolymerize lignin, but the ability of bacteria to react with this substrate remains elusive. We have therefore focused on elucidating strategies used by lignin-reactive soil bacteria and describing their oxidative enzyme systems. We now report the identification and characterization of an unusual C-type dye-decolorizing peroxidase from Amycolatopsis sp. 75iv2 (DyP2), which belongs to a family of heme peroxidases reported to be involved in bacterial lignin degradation. Biochemical studies indicate that DyP2 has novel function for this family, with versatile and high activity both as a peroxidase and Mn peroxidase (k(cat)/K(M) approximately 10(5)-10(6) M(-1) s(-1)). It also has a Mn-dependent oxidase mode of action that expands its substrate scope. Crystallographic studies of DyP2 at 2.25 A resolution show the existence of a Mn binding pocket and support its key role in catalysis.
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Identification and Characterization of a Multifunctional Dye Peroxidase from a Lignin-Reactive Bacterium.,Brown ME, Barros T, Chang MC ACS Chem Biol. 2012 Oct 10. PMID:23054399<ref>PMID:23054399</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Amycolatopsis sp. atcc 39116]]
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[[Category: Amycolatopsis sp. ATCC 39116]]
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[[Category: Barros, T]]
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[[Category: Large Structures]]
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[[Category: Brown, M E]]
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[[Category: Barros T]]
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[[Category: Chang, M C.Y]]
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[[Category: Brown ME]]
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[[Category: Dye peroxidase]]
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[[Category: Chang MCY]]
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[[Category: Oxidoreductase]]
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Current revision

DyP2 from Amycolatopsis sp. ATCC 39116

PDB ID 4g2c

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