6hqi: Difference between revisions
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<StructureSection load='6hqi' size='340' side='right'caption='[[6hqi]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='6hqi' size='340' side='right'caption='[[6hqi]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6hqi]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HQI OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6hqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HQI FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr id=' | <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>, <scene name='pdbligand=O:OXYGEN+ATOM'>O</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6hqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hqi OCA], [https://pdbe.org/6hqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hqi RCSB], [https://www.ebi.ac.uk/pdbsum/6hqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hqi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/PPOA_SOLLC PPOA_SOLLC] Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6hqi" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6hqi" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Tyrosinase 3D structures|Tyrosinase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Solanum lycopersicum]] | ||
[[Category: | [[Category: Bijelic A]] | ||
[[Category: Kampatsikas I]] | |||
[[Category: | [[Category: Rompel A]] | ||
[[Category: | |||
Latest revision as of 14:37, 24 January 2024
holo-form of polyphenol oxidase from Solanum lycopersicumholo-form of polyphenol oxidase from Solanum lycopersicum
Structural highlights
FunctionPPOA_SOLLC Catalyzes the oxidation of mono- and o-diphenols to o-diquinones. Publication Abstract from PubMedPolyphenol oxidases (PPOs) contain the structurally similar enzymes tyrosinases (TYRs) and catechol oxidases (COs). Two cDNAs encoding pro-PPOs from tomato (Solanum lycopersicum) were cloned and heterologously expressed in Escherichia coli. The two pro-PPOs (SlPPO1-2) differ remarkably in their activity as SlPPO1 reacts with the monophenols tyramine (kcat = 7.94 s(-1)) and phloretin (kcat = 2.42 s(-1)) and was thus characterized as TYR, whereas SlPPO2 accepts only diphenolic substrates like dopamine (kcat = 1.99 s(-1)) and caffeic acid (kcat = 20.33 s(-1)) rendering this enzyme a CO. This study, for the first time, characterizes a plant TYR and CO originating from the same organism. Moreover, X-ray structure analysis of the latent holo- and apo-SlPPO1 (PDB: 6HQI and 6HQJ) reveals an unprecedented high flexibility of the gatekeeper residue phenylalanine (Phe270). Docking studies showed that depending on its orientation the gatekeeper residue could either stabilize and correctly position incoming substrates or hinder their entrance into the active site. Furthermore, phloretin, a substrate of SIPPO1 (Km = 0.11 mM), is able to approach the active centre of SlPPO1 with both phenolic rings. Kinetic and structural results indicate that phloretin could act as a natural substrate and connote the participation of PPOs in flavonoid-biosynthesis. Biochemical and structural characterization of tomato polyphenol oxidases provide novel insights into their substrate specificity.,Kampatsikas I, Bijelic A, Rompel A Sci Rep. 2019 Mar 11;9(1):4022. doi: 10.1038/s41598-019-39687-0. PMID:30858490[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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