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6elv

From Proteopedia

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<StructureSection load='6elv' size='340' side='right'caption='[[6elv]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
<StructureSection load='6elv' size='340' side='right'caption='[[6elv]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6elv]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6elv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Malus_domestica Malus domestica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ELV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.05&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6els|6els]], [[6elt|6elt]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<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=6elv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elv OCA], [http://pdbe.org/6elv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6elv RCSB], [http://www.ebi.ac.uk/pdbsum/6elv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6elv ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6elv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elv OCA], [https://pdbe.org/6elv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6elv RCSB], [https://www.ebi.ac.uk/pdbsum/6elv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6elv ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/PPO_MALDO PPO_MALDO] Catalyzes the oxidation of mono- and o-diphenols to o-diquinones.
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The conversion of inactive pro-polyphenol oxidases (pro-PPOs) to the active enzyme results from the proteolytic cleavage of its C-terminal domain. Herein, a peptide mediated cleavage process that activates pro-MdPPO1 (Malus domestica) is reported. Mass spectrometry, mutagenesis studies and X-ray crystal structure analysis of pro-MdPPO1 (1.35 A) and two separated C-terminal domains, one obtained upon self-cleavage (Ccleaved) of the pro-MdPPO1 (1.35 A) and a second one produced independently (Csole) (1.05 A), were applied to identify the structural features for the observed self-cleavage. The results reveal that the sequence Lys355-Val370 located in the linker between the active and the C-terminal domain is indispensable for the self-cleaving as a mutant lacking this peptide did not undergo self-cleavage. Partial introduction (Lys352-Ala360) of this peptide into the sequence of two PPOs, MdPPO2 and aurone synthase (CgAUS1) triggered self-cleavage in the resulting mutants. This is the first experimental proof of a self-cleavage inducing peptide in PPOs unveiling a novel mode of activation for this enzyme class that is independent of any external protease.
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A peptide inducing self-cleavage reaction initiates the activation of tyrosinase.,Kampatsikas I, Bijelic A, Pretzler M, Rompel A Angew Chem Int Ed Engl. 2019 Mar 2. doi: 10.1002/anie.201901332. PMID:30825403<ref>PMID:30825403</ref>
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==See Also==
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*[[Tyrosinase 3D structures|Tyrosinase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6elv" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bijelic, A]]
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[[Category: Malus domestica]]
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[[Category: Kampatsikas, I]]
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[[Category: Bijelic A]]
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[[Category: Pretzler, M]]
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[[Category: Kampatsikas I]]
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[[Category: Rompel, A]]
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[[Category: Pretzler M]]
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[[Category: Autolysis]]
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[[Category: Rompel A]]
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[[Category: C-temrinal domain]]
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[[Category: Oxidoreductase]]
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[[Category: Polyphenol oxidase]]
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[[Category: Tyrosinase]]
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Current revision

Recombinantly expressed C-terminal domain of MdPPO1 (Csole-domain)

PDB ID 6elv

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