4h24

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{{STRUCTURE_4h24| PDB=4h24 | SCENE= }}
 
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===Cytochrome P450BM3-CIS cyclopropanation catalyst===
 
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{{ABSTRACT_PUBMED_23792734}}
 
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==Function==
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==Cytochrome P450BM3-CIS cyclopropanation catalyst==
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[[http://www.uniprot.org/uniprot/CPXB_BACME CPXB_BACME]] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
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<StructureSection load='4h24' size='340' side='right'caption='[[4h24]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4h24]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H24 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h24 OCA], [https://pdbe.org/4h24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h24 RCSB], [https://www.ebi.ac.uk/pdbsum/4h24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h24 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450BM3 gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state FeIII-to-FeII reduction potential and substantially improves NAD(P)H-driven activity.
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==About this Structure==
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A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo.,Coelho PS, Wang ZJ, Ener ME, Baril SA, Kannan A, Arnold FH, Brustad EM Nat Chem Biol. 2013 Jun 23. doi: 10.1038/nchembio.1278. PMID:23792734<ref>PMID:23792734</ref>
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[[4h24]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H24 OCA].
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==See Also==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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*[[Cytochrome P450|Cytochrome P450]]
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</div>
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*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
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<div class="pdbe-citations 4h24" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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<ref group="xtra">PMID:023792734</ref><references group="xtra"/><references/>
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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[[Category: Atcc 14581]]
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== References ==
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[[Category: Unspecific monooxygenase]]
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<references/>
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[[Category: Arnold, F H.]]
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__TOC__
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[[Category: Baril, S A.]]
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</StructureSection>
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[[Category: Brustad, E M.]]
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[[Category: Large Structures]]
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[[Category: Coelho, P S.]]
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[[Category: Priestia megaterium]]
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[[Category: Ener, M E.]]
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[[Category: Arnold FH]]
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[[Category: Kannan, A.]]
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[[Category: Baril SA]]
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[[Category: Wang, Z J.]]
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[[Category: Brustad EM]]
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[[Category: Cytochrome p450]]
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[[Category: Coelho PS]]
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[[Category: Directed evolution]]
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[[Category: Ener ME]]
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[[Category: Enzymatic cyclopropanation]]
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[[Category: Kannan A]]
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[[Category: Non-natural function]]
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[[Category: Wang ZJ]]
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[[Category: Oxidoreductase]]
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Current revision

Cytochrome P450BM3-CIS cyclopropanation catalyst

PDB ID 4h24

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