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| | <StructureSection load='3gyr' size='340' side='right'caption='[[3gyr]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3gyr' size='340' side='right'caption='[[3gyr]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gyr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"actinomyces_antibioticus"_waksman_and_woodruff_1941 "actinomyces antibioticus" waksman and woodruff 1941]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2g23 2g23]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GYR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gyr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2g23 2g23]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GYR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GYR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2g23|2g23]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C2O:CU-O-CU+LINKAGE'>C2O</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phsA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1890 "Actinomyces antibioticus" Waksman and Woodruff 1941])</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=3gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gyr OCA], [https://pdbe.org/3gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gyr RCSB], [https://www.ebi.ac.uk/pdbsum/3gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gyr ProSAT]</span></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=3gyr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gyr OCA], [https://pdbe.org/3gyr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gyr RCSB], [https://www.ebi.ac.uk/pdbsum/3gyr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gyr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PHSA_STRAT PHSA_STRAT]] Could be involved in the spore pigmentation and melanin production. Catalyzes the oxidative coupling of 2-aminophenols to form the 2-aminophenoxazinone chromophore. 2-aminophenoxazinone synthesis proceeds via a sequence of three consecutive 2-electron aminophenol oxidations. First, the o-aminophenol is oxidized by two electrons to the quinone imine, which then conjugates to a second o-aminophenol molecule while still bound to the enzyme. This product is further oxidized by two electrons to give rise to the p-quinone imine. The last two steps of the reaction, another conjugation to generate the tricyclic structure and a final two-electron oxidation to yield the 2-aminophenoxazinone product, are thought to be non-enzymatic. It can also uuse 3-hydroxyanthranilic acid (HAA), 4-methyl-3-hydroxyanthranilic acid (MHA), 3,4-dihydroxy-L-phenylalanine (L-DOPA), ferrocyanide and thiophenol as substrates.<ref>PMID:10770769</ref> <ref>PMID:2477054</ref> <ref>PMID:4118295</ref> <ref>PMID:19268377</ref>
| + | [https://www.uniprot.org/uniprot/PHSA_STRAT PHSA_STRAT] Could be involved in the spore pigmentation and melanin production. Catalyzes the oxidative coupling of 2-aminophenols to form the 2-aminophenoxazinone chromophore. 2-aminophenoxazinone synthesis proceeds via a sequence of three consecutive 2-electron aminophenol oxidations. First, the o-aminophenol is oxidized by two electrons to the quinone imine, which then conjugates to a second o-aminophenol molecule while still bound to the enzyme. This product is further oxidized by two electrons to give rise to the p-quinone imine. The last two steps of the reaction, another conjugation to generate the tricyclic structure and a final two-electron oxidation to yield the 2-aminophenoxazinone product, are thought to be non-enzymatic. It can also uuse 3-hydroxyanthranilic acid (HAA), 4-methyl-3-hydroxyanthranilic acid (MHA), 3,4-dihydroxy-L-phenylalanine (L-DOPA), ferrocyanide and thiophenol as substrates.<ref>PMID:10770769</ref> <ref>PMID:2477054</ref> <ref>PMID:4118295</ref> <ref>PMID:19268377</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces antibioticus waksman and woodruff 1941]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Allen, J P]] | + | [[Category: Streptomyces antibioticus]] |
| - | [[Category: Camara-Artigas, A]] | + | [[Category: Allen JP]] |
| - | [[Category: Francisco, W A]] | + | [[Category: Camara-Artigas A]] |
| - | [[Category: Smith, A W]] | + | [[Category: Francisco WA]] |
| - | [[Category: Wang, M]] | + | [[Category: Smith AW]] |
| - | [[Category: Antibiotic biosynthesis]]
| + | [[Category: Wang M]] |
| - | [[Category: Hexamer]]
| + | |
| - | [[Category: Laccase]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Metalloprotein]]
| + | |
| - | [[Category: Multicopper oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PHSA_STRAT Could be involved in the spore pigmentation and melanin production. Catalyzes the oxidative coupling of 2-aminophenols to form the 2-aminophenoxazinone chromophore. 2-aminophenoxazinone synthesis proceeds via a sequence of three consecutive 2-electron aminophenol oxidations. First, the o-aminophenol is oxidized by two electrons to the quinone imine, which then conjugates to a second o-aminophenol molecule while still bound to the enzyme. This product is further oxidized by two electrons to give rise to the p-quinone imine. The last two steps of the reaction, another conjugation to generate the tricyclic structure and a final two-electron oxidation to yield the 2-aminophenoxazinone product, are thought to be non-enzymatic. It can also uuse 3-hydroxyanthranilic acid (HAA), 4-methyl-3-hydroxyanthranilic acid (MHA), 3,4-dihydroxy-L-phenylalanine (L-DOPA), ferrocyanide and thiophenol as substrates.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the penultimate step in the biosynthesis of the antibiotic actinomycin D by Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric form and a hexameric form, with older actinomycin-producing cultures containing predominately the hexameric form. The structure of hexameric PHS has been determined using X-ray diffraction to a resolution limit of 2.30 A and is found to contain several unexpected and distinctive features. The structure forms a hexameric ring that is centered on a pseudo 6-fold axis and has an outer diameter of 185 A with a large central cavity that has a diameter of 50 A. This hexameric structure is stabilized by a long loop connecting two domains; bound to this long loop is a fifth copper atom that is present as a type 2 copper. This copper atom is not present in any other multicopper oxidase, and its presence appears to stabilize the hexameric structure.
Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center.,Smith AW, Camara-Artigas A, Wang M, Allen JP, Francisco WA Biochemistry. 2006 Apr 11;45(14):4378-87. PMID:16584173[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jones GH. Actinomycin production persists in a strain of Streptomyces antibioticus lacking phenoxazinone synthase. Antimicrob Agents Chemother. 2000 May;44(5):1322-7. PMID:10770769
- ↑ Barry CE 3rd, Nayar PG, Begley TP. Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin. Biochemistry. 1989 Jul 25;28(15):6323-33. PMID:2477054
- ↑ Golub EE, Nishimura JS. Phenoxazinone synthetase from Streptomyces antibioticus: multiple activities of the enzyme. J Bacteriol. 1972 Dec;112(3):1353-7. PMID:4118295
- ↑ Le Roes-Hill M, Goodwin C, Burton S. Phenoxazinone synthase: what's in a name? Trends Biotechnol. 2009 Apr;27(4):248-58. doi: 10.1016/j.tibtech.2009.01.001., Epub 2009 Mar 4. PMID:19268377 doi:http://dx.doi.org/10.1016/j.tibtech.2009.01.001
- ↑ Smith AW, Camara-Artigas A, Wang M, Allen JP, Francisco WA. Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center. Biochemistry. 2006 Apr 11;45(14):4378-87. PMID:16584173 doi:10.1021/bi0525526
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