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| | ==Latent aurone synthase (polyphenol oxidase) from natural source== | | ==Latent aurone synthase (polyphenol oxidase) from natural source== |
| - | <StructureSection load='4z11' size='340' side='right' caption='[[4z11]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='4z11' size='340' side='right'caption='[[4z11]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4z11]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Coreopsis_grandiflora Coreopsis grandiflora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z11 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z11 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4z11]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Coreopsis_grandiflora Coreopsis grandiflora]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z11 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene></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=4z11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z11 OCA], [http://pdbe.org/4z11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z11 RCSB], [http://www.ebi.ac.uk/pdbsum/4z11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4z11 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=4z11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z11 OCA], [https://pdbe.org/4z11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z11 RCSB], [https://www.ebi.ac.uk/pdbsum/4z11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z11 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A075DN54_CORGR A0A075DN54_CORGR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Coreopsis grandiflora]] | | [[Category: Coreopsis grandiflora]] |
| - | [[Category: Mauracher, S G]] | + | [[Category: Large Structures]] |
| - | [[Category: Molitor, C]] | + | [[Category: Mauracher SG]] |
| - | [[Category: Rompel, A]] | + | [[Category: Molitor C]] |
| - | [[Category: Aurone synthase]] | + | [[Category: Rompel A]] |
| - | [[Category: Latent]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Polyphenol oxidase]]
| + | |
| - | [[Category: Type iii copper protein]]
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| Structural highlights
Function
A0A075DN54_CORGR
Publication Abstract from PubMed
Tyrosinases and catechol oxidases belong to the family of polyphenol oxidases (PPOs). Tyrosinases catalyze theo-hydroxylation and oxidation of phenolic compounds, whereas catechol oxidases were so far defined to lack the hydroxylation activity and catalyze solely the oxidation ofo-diphenolic compounds. Aurone synthase fromCoreopsis grandiflora(AUS1) is a specialized plant PPO involved in the anabolic pathway of aurones. We present, to our knowledge, the first crystal structures of a latent plant PPO, its mature active and inactive form, caused by a sulfation of a copper binding histidine. Analysis of the latent proenzyme's interface between the shielding C-terminal domain and the main core provides insights into its activation mechanisms. As AUS1 did not accept common tyrosinase substrates (tyrosine and tyramine), the enzyme is classified as a catechol oxidase. However, AUS1 showed hydroxylase activity toward its natural substrate (isoliquiritigenin), revealing that the hydroxylase activity is not correlated with the acceptance of common tyrosinase substrates. Therefore, we propose that the hydroxylase reaction is a general functionality of PPOs. Molecular dynamics simulations of docked substrate-enzyme complexes were performed, and a key residue was identified that influences the plant PPO's acceptance or rejection of tyramine. Based on the evidenced hydroxylase activity and the interactions of specific residues with the substrates during the molecular dynamics simulations, a novel catalytic reaction mechanism for plant PPOs is proposed. The presented results strongly suggest that the physiological role of plant catechol oxidases were previously underestimated, as they might hydroxylate their-so far unknown-natural substrates in vivo.
Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases.,Molitor C, Mauracher SG, Rompel A Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):E1806-15. doi:, 10.1073/pnas.1523575113. Epub 2016 Mar 14. PMID:26976571[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Molitor C, Mauracher SG, Rompel A. Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases. Proc Natl Acad Sci U S A. 2016 Mar 29;113(13):E1806-15. doi:, 10.1073/pnas.1523575113. Epub 2016 Mar 14. PMID:26976571 doi:http://dx.doi.org/10.1073/pnas.1523575113
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