5xa3: Difference between revisions

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-'''Unreleased structure'''
-The entry 5xa3 is ON HOLD  until Paper Publication
+==Crystal Structure of P450BM3 with Benzyloxycarbonyl-L-prolyl-L-phenylalanine==
+<StructureSection load='5xa3' size='340' side='right'caption='[[5xa3]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5xa3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium_NBRC_15308_=_ATCC_14581 Priestia megaterium NBRC 15308 = ATCC 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XA3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XA3 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]] 2.2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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=5xa3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xa3 OCA], [https://pdbe.org/5xa3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xa3 RCSB], [https://www.ebi.ac.uk/pdbsum/5xa3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xa3 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CPXB_PRIM2 CPXB_PRIM2] Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).<ref>PMID:11695892</ref> <ref>PMID:14653735</ref> <ref>PMID:16403573</ref> <ref>PMID:16566047</ref> <ref>PMID:17077084</ref> <ref>PMID:1727637</ref> <ref>PMID:17868686</ref> <ref>PMID:18004886</ref> <ref>PMID:18020460</ref> <ref>PMID:18298086</ref> <ref>PMID:18619466</ref> <ref>PMID:18721129</ref> <ref>PMID:19492389</ref> <ref>PMID:20180779</ref> <ref>PMID:21110374</ref> <ref>PMID:21875028</ref> <ref>PMID:3106359</ref> <ref>PMID:7578081</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The selective hydroxylation of benzene to phenol, without the formation of side products resulting from overoxidation, is catalyzed by cytochrome P450BM3 with the assistance of amino acid derivatives as decoy molecules. The catalytic turnover rate and the total turnover number reached 259 min(-1) P450BM3(-1) and 40 200 P450BM3(-1) when N-heptyl-l-proline modified with l-phenylalanine (C7-l-Pro-l-Phe) was used as the decoy molecule. This work shows that amino acid derivatives with a totally different structure from fatty acids can be used as decoy molecules for aromatic hydroxylation by wild-type P450BM3. This method for non-native substrate hydroxylation by wild-type P450BM3 has the potential to expand the utility of P450BM3 for biotransformations.
-Authors: Shoji, O., Yanagisawa, S., Stanfield, J.K., Suzuki, K., Kasai, C., Cong, Z., Sugimoto, H., Shiro, Y., Watanabe, Y.
+Direct Hydroxylation of Benzene to Phenol by Cytochrome P450BM3 Triggered by Amino Acid Derivatives.,Shoji O, Yanagisawa S, Stanfield JK, Suzuki K, Cong Z, Sugimoto H, Shiro Y, Watanabe Y Angew Chem Int Ed Engl. 2017 Aug 21;56(35):10324-10329. doi:, 10.1002/anie.201703461. Epub 2017 Jun 8. PMID:28544674<ref>PMID:28544674</ref>
-Description: Crystal Structure of P450BM3 with Benzyloxycarbonyl-L-prolyl-L-phenylalanine
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Shiro, Y]]
+<div class="pdbe-citations 5xa3" style="background-color:#fffaf0;"></div>
-[[Category: Sugimoto, H]]
-[[Category: Yanagisawa, S]]
+==See Also==
-[[Category: Shoji, O]]
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
-[[Category: Suzuki, K]]
+== References ==
-[[Category: Kasai, C]]
+<references/>
-[[Category: Stanfield, J.K]]
+__TOC__
-[[Category: Watanabe, Y]]
+</StructureSection>
-[[Category: Cong, Z]]
+[[Category: Large Structures]]
+[[Category: Priestia megaterium NBRC 15308 = ATCC 14581]]
+[[Category: Cong Z]]
+[[Category: Kasai C]]
+[[Category: Shiro Y]]
+[[Category: Shoji O]]
+[[Category: Stanfield JK]]
+[[Category: Sugimoto H]]
+[[Category: Suzuki K]]
+[[Category: Watanabe Y]]
+[[Category: Yanagisawa S]]