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==Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with guaiacol.==
==Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with guaiacol.==
<StructureSection load='5ncb' size='340' side='right' caption='[[5ncb]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
<StructureSection load='5ncb' size='340' side='right'caption='[[5ncb]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5ncb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NCB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NCB FirstGlance]. <br>
<table><tr><td colspan='2'>[[5ncb]] is a 1 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=5NCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NCB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=JZ3:GUAIACOL'>JZ3</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.44&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=JZ3:GUAIACOL'>JZ3</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5ncb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ncb OCA], [http://pdbe.org/5ncb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ncb RCSB], [http://www.ebi.ac.uk/pdbsum/5ncb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ncb 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=5ncb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ncb OCA], [https://pdbe.org/5ncb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ncb RCSB], [https://www.ebi.ac.uk/pdbsum/5ncb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ncb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A076MY51_AMYME A0A076MY51_AMYME]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microbial aromatic catabolism offers a promising approach to convert lignin, a vast source of renewable carbon, into useful products. Aryl-O-demethylation is an essential biochemical reaction to ultimately catabolize coniferyl and sinapyl lignin-derived aromatic compounds, and is often a key bottleneck for both native and engineered bioconversion pathways. Here, we report the comprehensive characterization of a promiscuous P450 aryl-O-demethylase, consisting of a cytochrome P450 protein from the family CYP255A (GcoA) and a three-domain reductase (GcoB) that together represent a new two-component P450 class. Though originally described as converting guaiacol to catechol, we show that this system efficiently demethylates both guaiacol and an unexpectedly wide variety of lignin-relevant monomers. Structural, biochemical, and computational studies of this novel two-component system elucidate the mechanism of its broad substrate specificity, presenting it as a new tool for a critical step in biological lignin conversion.
A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion.,Mallinson SJB, Machovina MM, Silveira RL, Garcia-Borras M, Gallup N, Johnson CW, Allen MD, Skaf MS, Crowley MF, Neidle EL, Houk KN, Beckham GT, DuBois JL, McGeehan JE Nat Commun. 2018 Jun 27;9(1):2487. doi: 10.1038/s41467-018-04878-2. PMID:29950589<ref>PMID:29950589</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ncb" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beckham, G T]]
[[Category: Amycolatopsis sp. ATCC 39116]]
[[Category: Johnson, C W]]
[[Category: Large Structures]]
[[Category: Mallinson, S J.B]]
[[Category: Beckham GT]]
[[Category: McGeehan, J E]]
[[Category: Johnson CW]]
[[Category: Neidle, E L]]
[[Category: Mallinson SJB]]
[[Category: Amycolatopsis]]
[[Category: McGeehan JE]]
[[Category: Cyp255a]]
[[Category: Neidle EL]]
[[Category: Cytochrome]]
[[Category: Guaiacol]]
[[Category: Haem]]
[[Category: Heme]]
[[Category: Lignin]]
[[Category: Oxidoreductase]]
[[Category: P450]]
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