8hgt
From Proteopedia
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(New page: '''Unreleased structure''' The entry 8hgt is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the CYP153A mutant V456A from Marinobacter aquaeolei== | |
| + | <StructureSection load='8hgt' size='340' side='right'caption='[[8hgt]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinobacter_nauticus Marinobacter nauticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HGT 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]] 2.06Å</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></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=8hgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hgt OCA], [https://pdbe.org/8hgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hgt RCSB], [https://www.ebi.ac.uk/pdbsum/8hgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hgt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A368UNN3_MARNT A0A368UNN3_MARNT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Given prominent physicochemical similarities between H(2)O(2) and water, we report a new strategy for promoting the peroxygenase activity of P450 enzymes by engineering their water tunnels to facilitate H(2)O(2) access to the heme center buried therein. Specifically, the H(2)O(2)-driven activities of two native NADH-dependent P450 enzymes (CYP199A4 and CYP153A(M.aq)) increase significantly (by >183-fold and >15-fold, respectively). Additionally, the amount of H(2)O(2) required for an artificial P450 peroxygenase facilitated by a dual-functional small molecule to obtain the desired product is reduced by 95%-97.5% (with approximately 95% coupling efficiency). Structural analysis suggests that mutating the residue at the bottleneck of the water tunnel may open a second pathway for H(2)O(2) to flow to the heme center (in addition to the natural substrate tunnel). This study highlights a promising, generalizable strategy whereby P450 monooxygenases can be modified to adopt peroxygenase activity through H(2)O(2) tunnel engineering, thus broadening the application scope of P450s in synthetic chemistry and synthetic biology. | ||
| - | + | Enabling Peroxygenase Activity in Cytochrome P450 Monooxygenases by Engineering Hydrogen Peroxide Tunnels.,Zhao P, Kong F, Jiang Y, Qin X, Tian X, Cong Z J Am Chem Soc. 2023 Mar 8;145(9):5506-5511. doi: 10.1021/jacs.3c00195. Epub 2023 , Feb 15. PMID:36790023<ref>PMID:36790023</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8hgt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Marinobacter nauticus]] | ||
| + | [[Category: Cong Z]] | ||
| + | [[Category: Jiang Y]] | ||
| + | [[Category: Tian X]] | ||
Current revision
Crystal structure of the CYP153A mutant V456A from Marinobacter aquaeolei
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