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4l54

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==Structure of cytochrome P450 OleT, ligand-free==
==Structure of cytochrome P450 OleT, ligand-free==
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<StructureSection load='4l54' size='340' side='right' caption='[[4l54]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4l54' size='340' side='right'caption='[[4l54]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4l54]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Jeotgalicoccus_sp._atcc_8456 Jeotgalicoccus sp. atcc 8456]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L54 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L54 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4l54]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Jeotgalicoccus_sp._ATCC_8456 Jeotgalicoccus sp. ATCC 8456]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4L54 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene><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]] 2.3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l40|4l40]]</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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l54 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l54 RCSB], [http://www.ebi.ac.uk/pdbsum/4l54 PDBsum]</span></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=4l54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l54 OCA], [https://pdbe.org/4l54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4l54 RCSB], [https://www.ebi.ac.uk/pdbsum/4l54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4l54 ProSAT]</span></td></tr>
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<table>
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</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/E9NSU2_9STAP E9NSU2_9STAP]
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The production of hydrocarbons in nature has been documented for only a limited set of organisms, with many of the molecular components underpinning these processes only recently identified. There is an obvious scope for application of these catalysts and engineered variants thereof in the future production of biofuels. Here we present biochemical characterization and crystal structures of a cytochrome P450 fatty acid peroxygenase: the terminal alkene forming OleTJE (CYP152L1) from Jeotgalicoccus sp. 8456. OleTJE is stabilized at high ionic strength, but aggregation and precipitation of OleTJE in low salt buffer can be turned to advantage for purification, because resolubilized OleTJE is fully active and extensively dissociated from lipids. OleTJE binds avidly to a range of long chain fatty acids, and structures of both ligand-free and arachidic acid-bound OleTJE reveal that the P450 active site is preformed for fatty acid binding. OleTJE heme iron has an unusually positive redox potential (-103 mV versus normal hydrogen electrode), which is not significantly affected by substrate binding, despite extensive conversion of the heme iron to a high spin ferric state. Terminal alkenes are produced from a range of saturated fatty acids (C12-C20), and stopped-flow spectroscopy indicates a rapid reaction between peroxide and fatty acid-bound OleTJE (167 s(-1) at 200 mum H2O2). Surprisingly, the active site is highly similar in structure to the related P450BSbeta, which catalyzes hydroxylation of fatty acids as opposed to decarboxylation. Our data provide new insights into structural and mechanistic properties of a robust P450 with potential industrial applications.
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Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium.,Belcher J, McLean KJ, Matthews S, Woodward LS, Fisher K, Rigby SE, Nelson DR, Potts D, Baynham MT, Parker DA, Leys D, Munro AW J Biol Chem. 2014 Mar 7;289(10):6535-50. doi: 10.1074/jbc.M113.527325. Epub 2014 , Jan 18. PMID:24443585<ref>PMID:24443585</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Jeotgalicoccus sp. atcc 8456]]
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[[Category: Jeotgalicoccus sp. ATCC 8456]]
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[[Category: Leys, D.]]
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[[Category: Large Structures]]
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[[Category: Decarboxylase]]
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[[Category: Leys D]]
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[[Category: Oxidoreductase]]
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[[Category: Peroxidase]]
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Current revision

Structure of cytochrome P450 OleT, ligand-free

PDB ID 4l54

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