5zlh

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Current revision (10:28, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5zlh' size='340' side='right'caption='[[5zlh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='5zlh' size='340' side='right'caption='[[5zlh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zlh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZLH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ZLH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zlh]] 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=5ZLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZLH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNH:MANGANESE+PROTOPORPHYRIN+IX'>MNH</scene></td></tr>
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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]] 3.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5zis|5zis]]</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=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://proteopedia.org/fgij/fg.htm?mol=5zlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zlh OCA], [http://pdbe.org/5zlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zlh RCSB], [http://www.ebi.ac.uk/pdbsum/5zlh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zlh ProSAT]</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=5zlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zlh OCA], [https://pdbe.org/5zlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zlh RCSB], [https://www.ebi.ac.uk/pdbsum/5zlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zlh ProSAT]</span></td></tr>
</table>
</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/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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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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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5zlh" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Aiba, Y]]
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[[Category: Priestia megaterium]]
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[[Category: Omura, K]]
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[[Category: Aiba Y]]
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[[Category: Onoda, H]]
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[[Category: Omura K]]
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[[Category: Shoji, O]]
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[[Category: Onoda H]]
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[[Category: Sugimoto, H]]
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[[Category: Shoji O]]
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[[Category: Watanabe, Y]]
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[[Category: Sugimoto H]]
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[[Category: Cytochrome p450]]
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[[Category: Watanabe Y]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal structure of Mn-ProtoporphyrinIX-reconstituted P450BM3

PDB ID 5zlh

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