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| | <StructureSection load='5de9' size='340' side='right'caption='[[5de9]], [[Resolution|resolution]] 1.76Å' scene=''> | | <StructureSection load='5de9' size='340' side='right'caption='[[5de9]], [[Resolution|resolution]] 1.76Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5de9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3tnk 3tnk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DE9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DE9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5de9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3tnk 3tnk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DE9 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr> | + | </td></tr><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>, <scene name='pdbligand=SPM:SPERMINE'>SPM</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cyp158a2, SCO1207 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 "Actinomyces coelicolor" (Muller 1908) Lieske 1921])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5de9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5de9 OCA], [https://pdbe.org/5de9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5de9 RCSB], [https://www.ebi.ac.uk/pdbsum/5de9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5de9 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Biflaviolin_synthase Biflaviolin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.21.7 1.14.21.7] </span></td></tr>
| + | |
| - | <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=5de9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5de9 OCA], [http://pdbe.org/5de9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5de9 RCSB], [http://www.ebi.ac.uk/pdbsum/5de9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5de9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/C1582_STRCO C1582_STRCO]] Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).<ref>PMID:15659395</ref> <ref>PMID:16239228</ref> | + | [https://www.uniprot.org/uniprot/C1582_STRCO C1582_STRCO] Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).<ref>PMID:15659395</ref> <ref>PMID:16239228</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Biflaviolin synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Zhao, B]] | + | [[Category: Streptomyces coelicolor]] |
| - | [[Category: Cyp158a2]] | + | [[Category: Zhao B]] |
| - | [[Category: Cytochrome p450]]
| + | |
| - | [[Category: Oxidative coupling reaction]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
C1582_STRCO Catalyze oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments which protect the soil bacterium from deleterious effects of UV irradiation (three isomers of biflaviolin and one triflaviolin).[1] [2]
Publication Abstract from PubMed
Both CYP158A1 and CYP158A2 are able to catalyze an oxidative C-C coupling reaction producing biflaviolin or triflaviolin in Streptomyces coelicolor A3(2). The substrate-bound crystal structures of CYP158A2 and CYP158A1 reveal that the side chain of Ile87 in CYP158A2 points to the active site contacting the distal flaviolin molecule, however, the bulkier side chain of Lys90 in CYP158A1 (corresponding to Ile87 in CYP158A2) is toward the distal surface of the protein. These results suggest that these residues could be important in determining product regiospecificity. In order to explore the role of the two residues in catalysis, the reciprocal mutants, Ile87Lys and Lys90Ile, of CYP158A2 and CYP158A1, respectively, were generated and characterized. The mutant Ile87Lys enzyme forms two isomers of biflaviolin instead of three isomers of biflaviolin in wild-type CYP158A2. CYP158A1 containing the substitution of lysine with isoleucine has the same catalytic activity compared with the wild-type CYP158A1. The crystal structure of Ile87Lys showed that the BC loop in the mutant is in a very different orientation compared with the BC loop in both CYP158A1/A2 structures. These results shed light on the mechanism of the oxidative coupling reaction catalyzed by cytochrome P450.
The role of Ile87 of CYP158A2 in oxidative coupling reaction.,Zhao B, Bellamine A, Lei L, Waterman MR Arch Biochem Biophys. 2011 Dec 19. PMID:22203090[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhao B, Guengerich FP, Bellamine A, Lamb DC, Izumikawa M, Lei L, Podust LM, Sundaramoorthy M, Kalaitzis JA, Reddy LM, Kelly SL, Moore BS, Stec D, Voehler M, Falck JR, Shimada T, Waterman MR. Binding of two flaviolin substrate molecules, oxidative coupling, and crystal structure of Streptomyces coelicolor A3(2) cytochrome P450 158A2. J Biol Chem. 2005 Mar 25;280(12):11599-607. Epub 2005 Jan 19. PMID:15659395 doi:http://dx.doi.org/10.1074/jbc.M410933200
- ↑ Zhao B, Guengerich FP, Voehler M, Waterman MR. Role of active site water molecules and substrate hydroxyl groups in oxygen activation by cytochrome P450 158A2: a new mechanism of proton transfer. J Biol Chem. 2005 Dec 23;280(51):42188-97. Epub 2005 Oct 20. PMID:16239228 doi:10.1074/jbc.M509220200
- ↑ Zhao B, Bellamine A, Lei L, Waterman MR. The role of Ile87 of CYP158A2 in oxidative coupling reaction. Arch Biochem Biophys. 2011 Dec 19. PMID:22203090 doi:10.1016/j.abb.2011.12.007
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