3cbd: Difference between revisions

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-{{Seed}}
-[[Image:3cbd.png|left|200px]]
-<!--
+==Directed Evolution of cytochrome P450 BM3, to octane monoxygenase 139-3==
-The line below this paragraph, containing "STRUCTURE_3cbd", creates the "Structure Box" on the page.
+<StructureSection load='3cbd' size='340' side='right'caption='[[3cbd]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3cbd]] is a 2 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=3CBD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CBD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=140:N-PALMITOYLGLYCINE'>140</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
-{{STRUCTURE_3cbd|  PDB=3cbd  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3cbd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cbd OCA], [https://pdbe.org/3cbd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3cbd RCSB], [https://www.ebi.ac.uk/pdbsum/3cbd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3cbd 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>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cb/3cbd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cbd ConSurf].
+<div style="clear:both"></div>
-===Directed Evolution of cytochrome P450 BM3, to octane monoxygenase 139-3===
+==See Also==
+*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
+*[[Escherichia coli LepA%2C the ribosomal back translocase|Escherichia coli LepA%2C the ribosomal back translocase]]
-<!--
+== References ==
-The line below this paragraph, {{ABSTRACT_PUBMED_18619466}}, adds the Publication Abstract to the page
+<references/>
-(as it appears on PubMed at http://www.pubmed.gov), where 18619466 is the PubMed ID number.
+__TOC__
--->
+</StructureSection>
-{{ABSTRACT_PUBMED_18619466}}
+[[Category: Large Structures]]
+[[Category: Priestia megaterium]]
-==About this Structure==
+[[Category: Li H]]
-CBD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CBD OCA].
+[[Category: Meharenna YT]]
+[[Category: Poulos TL]]
-==Reference==
-Evolutionary history of a specialized p450 propane monooxygenase., Fasan R, Meharenna YT, Snow CD, Poulos TL, Arnold FH, J Mol Biol. 2008 Nov 28;383(5):1069-80. Epub 2008 Jun 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18619466 18619466]
-[[Category: Bacillus megaterium]]
-[[Category: Single protein]]
-[[Category: Unspecific monooxygenase]]
-[[Category: Li, H.]]
-[[Category: Meharenna, Y T.]]
-[[Category: Poulos, T L.]]
-[[Category: Cytochrome p450]]
-[[Category: Electron transport]]
-[[Category: Fad]]
-[[Category: Flavoprotein]]
-[[Category: Fmn]]
-[[Category: Hemeprotein 139-3]]
-[[Category: Iron]]
-[[Category: Membrane]]
-[[Category: Metal-binding]]
-[[Category: Monooxygenase]]
-[[Category: Multifunctional enzyme]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]
-[[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov  5 10:39:14 2008''