2nnb

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(New page: 200px<br /><applet load="2nnb" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nnb, resolution 1.90&Aring;" /> '''The Q403K mutnat hem...)
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[[Image:2nnb.jpg|left|200px]]<br /><applet load="2nnb" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2nnb, resolution 1.90&Aring;" />
 
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'''The Q403K mutnat heme domain of flavocytochrome P450 BM3'''<br />
 
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==About this Structure==
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==The Q403K mutant heme domain of flavocytochrome P450 BM3==
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2NNB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NNB OCA].
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<StructureSection load='2nnb' size='340' side='right'caption='[[2nnb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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[[Category: Bacillus megaterium]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2nnb]] 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=2NNB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNB FirstGlance]. <br>
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[[Category: Unspecific monooxygenase]]
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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]] 1.9&#8491;</td></tr>
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[[Category: Anderson, J.L.R.]]
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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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[[Category: Chapman, S.K.]]
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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=2nnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnb OCA], [https://pdbe.org/2nnb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnb RCSB], [https://www.ebi.ac.uk/pdbsum/2nnb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnb ProSAT]</span></td></tr>
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[[Category: Clark, J.P.]]
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</table>
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[[Category: Miles, C.S.]]
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== Function ==
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[[Category: Mowat, C.G.]]
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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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[[Category: Reid, G.A.]]
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== Evolutionary Conservation ==
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[[Category: HEM]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: fatty-acid hydroxylase]]
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Check<jmol>
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[[Category: flavocytochrome p450]]
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<jmolCheckbox>
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[[Category: heme domain]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/2nnb_consurf.spt"</scriptWhenChecked>
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[[Category: oxidoreductase]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2nnb ConSurf].
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<div style="clear:both"></div>
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:48:29 2007''
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==See Also==
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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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: Large Structures]]
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[[Category: Priestia megaterium]]
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[[Category: Anderson JLR]]
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[[Category: Chapman SK]]
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[[Category: Clark JP]]
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[[Category: Miles CS]]
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[[Category: Mowat CG]]
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[[Category: Reid GA]]

Current revision

The Q403K mutant heme domain of flavocytochrome P450 BM3

PDB ID 2nnb

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