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3gyr
From Proteopedia
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| - | [[Image:3gyr.png|left|200px]] | ||
| - | + | ==Structure of Phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center.== | |
| + | <StructureSection load='3gyr' size='340' side='right'caption='[[3gyr]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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='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='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='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> | ||
| + | == 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> | ||
| + | == 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/gy/3gyr_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=3gyr ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:16584173</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3gyr" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | < | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
[[Category: Streptomyces antibioticus]] | [[Category: Streptomyces antibioticus]] | ||
| - | [[Category: Allen | + | [[Category: Allen JP]] |
| - | [[Category: Camara-Artigas | + | [[Category: Camara-Artigas A]] |
| - | [[Category: Francisco | + | [[Category: Francisco WA]] |
| - | [[Category: Smith | + | [[Category: Smith AW]] |
| - | [[Category: Wang | + | [[Category: Wang M]] |
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Current revision
Structure of Phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center.
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