1zoa

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[[Image:1zoa.png|left|200px]]
 
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{{STRUCTURE_1zoa| PDB=1zoa | SCENE= }}
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==Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine==
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<StructureSection load='1zoa' size='340' side='right'caption='[[1zoa]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zoa]] 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=1ZOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZOA FirstGlance]. <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]] 1.74&#8491;</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=140:N-PALMITOYLGLYCINE'>140</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=1zoa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zoa OCA], [https://pdbe.org/1zoa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zoa RCSB], [https://www.ebi.ac.uk/pdbsum/1zoa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zoa ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zoa_consurf.spt"</scriptWhenChecked>
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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=1zoa ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Identifying key structural features of cytochromes P450 is critical in understanding the catalytic mechanism of these important drug-metabolizing enzymes. Cytochrome P450BM-3 (BM-3), a structural and mechanistic P450 model, catalyzes the regio- and stereoselective hydroxylation of fatty acids. Recent work has demonstrated the importance of water in the mechanism of BM-3, and site-specific mutagenesis has helped to elucidate mechanisms of substrate recognition, binding, and product formation. One of the amino acids identified as playing a key role in the active site of BM-3 is alanine 328, which is located in the loop between the K helix and beta 1-4. In the A328V BM-3 mutant, substrate affinity increases 5-10-fold and the turnover number increases 2-8-fold compared to wild-type enzyme. Unlike wild-type enzyme, this mutant is purified from E. coli with endogenous substrate bound due to the higher binding affinity. Close examination of the crystal structures of the substrate-bound native and A328V mutant BMPs indicates that the positioning of the substrate is essentially identical in the two forms of the enzyme, with the two valine methyl groups occupying voids present in the active site of the wild-type substrate-bound structure.
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===Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine===
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A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation.,Haines DC, Hegde A, Chen B, Zhao W, Bondlela M, Humphreys JM, Mullin DA, Tomchick DR, Machius M, Peterson JA Biochemistry. 2011 Oct 4;50(39):8333-41. Epub 2011 Sep 6. PMID:21875028<ref>PMID:21875028</ref>
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{{ABSTRACT_PUBMED_21875028}}
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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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==About this Structure==
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<div class="pdbe-citations 1zoa" style="background-color:#fffaf0;"></div>
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[[1zoa]] is a 2 chain structure with 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=1ZOA OCA].
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==See Also==
==See Also==
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*[[NADPH-Cytochrome P450 Reductase|NADPH-Cytochrome P450 Reductase]]
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*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:021875028</ref><references group="xtra"/>
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__TOC__
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[[Category: Bacillus megaterium]]
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</StructureSection>
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[[Category: Unspecific monooxygenase]]
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[[Category: Large Structures]]
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[[Category: Bondlela, M.]]
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[[Category: Priestia megaterium]]
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[[Category: Chen, B.]]
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[[Category: Bondlela M]]
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[[Category: Graham, S E.]]
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[[Category: Chen B]]
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[[Category: Haines, D C.]]
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[[Category: Graham SE]]
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[[Category: Hegda, A.]]
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[[Category: Haines DC]]
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[[Category: Machius, M.]]
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[[Category: Hegda A]]
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[[Category: Mullin, D.]]
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[[Category: Machius M]]
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[[Category: Peterson, J A.]]
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[[Category: Mullin D]]
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[[Category: Tomchick, D R.]]
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[[Category: Peterson JA]]
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[[Category: Cytochrome p-450]]
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[[Category: Tomchick DR]]
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[[Category: Hemeprotein a328v]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure Of A328V Mutant Of The Heme Domain Of P450Bm-3 With N-Palmitoylglycine

PDB ID 1zoa

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