5omr: Difference between revisions
New page: '''Unreleased structure''' The entry 5omr is ON HOLD Authors: Mallinson, S.J.B., Johnson, C.W., Neidle, E.L., Beckham, G.T., McGeehan, J.E. Description: Crystal structure of Amycolatop... |
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==Crystal structure of Amycolatopsis cytochrome P450 GcoA in complex with vanillin.== | |||
<StructureSection load='5omr' size='340' side='right'caption='[[5omr]], [[Resolution|resolution]] 1.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5omr]] 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=5OMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OMR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.68Å</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=V55:4-HYDROXY-3-METHOXYBENZALDEHYDE'>V55</scene></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=5omr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5omr OCA], [https://pdbe.org/5omr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5omr RCSB], [https://www.ebi.ac.uk/pdbsum/5omr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5omr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A3B6UEE9_AMYS7 A0A3B6UEE9_AMYS7] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5omr" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Amycolatopsis sp. ATCC 39116]] | |||
[[Category: Large Structures]] | |||
[[Category: Beckham GT]] | |||
[[Category: Johnson CW]] | |||
[[Category: Mallinson SJB]] | |||
[[Category: McGeehan JE]] | |||
[[Category: Neidle EL]] |