8hgc: Difference between revisions
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==Crystal structure of the CYP199A4 mutant F182T in complex with 4-methoxybenzoic acid== | |||
<StructureSection load='8hgc' size='340' side='right'caption='[[8hgc]], [[Resolution|resolution]] 1.72Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8hgc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodopseudomonas_palustris_HaA2 Rhodopseudomonas palustris HaA2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HGC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HGC 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]] 1.72Å</td></tr> | |||
<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=ANN:4-METHOXYBENZOIC+ACID'>ANN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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=8hgc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hgc OCA], [https://pdbe.org/8hgc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hgc RCSB], [https://www.ebi.ac.uk/pdbsum/8hgc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hgc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q2IU02_RHOP2 Q2IU02_RHOP2] | |||
<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 8hgc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodopseudomonas palustris HaA2]] | |||
[[Category: Cong Z]] | |||
[[Category: Jiang Y]] | |||
