5zis

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'''Unreleased structure'''
 
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The entry 5zis is ON HOLD
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==Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3==
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<StructureSection load='5zis' size='340' side='right' caption='[[5zis]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5zis]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZIS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zis FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zis OCA], [http://pdbe.org/5zis PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zis RCSB], [http://www.ebi.ac.uk/pdbsum/5zis PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zis ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CPXB_BACMB CPXB_BACMB]] 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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Haem substitution is an effective approach to tweak the function of haemoproteins. Herein, we report a facile haem substitution method for self-sufficient cytochrome P450BM3 (CYP102A1) from Bacillus megaterium utilising the transpeptidase Sortase A from Staphylococcus aureus. We successfully constructed Mn-substituted BM3 and investigated its catalytic activity.
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Authors: Omura, K., Aiba, Y., Onoda, H., Sugimoto, H., Shoji, O., Watanabe, Y.
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Reconstitution of full-length P450BM3 with an artificial metal complex by utilising the transpeptidase Sortase A.,Omura K, Aiba Y, Onoda H, Stanfield JK, Ariyasu S, Sugimoto H, Shiro Y, Shoji O, Watanabe Y Chem Commun (Camb). 2018 Jul 12;54(57):7892-7895. doi: 10.1039/c8cc02760a. PMID:29845154<ref>PMID:29845154</ref>
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Description: Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5zis" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aiba, Y]]
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[[Category: Omura, K]]
[[Category: Onoda, H]]
[[Category: Onoda, H]]
[[Category: Shoji, O]]
[[Category: Shoji, O]]
[[Category: Sugimoto, H]]
[[Category: Sugimoto, H]]
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[[Category: Aiba, Y]]
 
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[[Category: Omura, K]]
 
[[Category: Watanabe, Y]]
[[Category: Watanabe, Y]]
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[[Category: Cytochrome p450]]
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[[Category: Oxidoreductase]]

Revision as of 16:09, 15 August 2018

Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3

5zis, resolution 3.10Å

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