6els: Difference between revisions
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==Structure of latent apple tyrosinase (MdPPO1)== | |||
<StructureSection load='6els' size='340' side='right'caption='[[6els]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6els]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELS 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>, <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6els FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6els OCA], [http://pdbe.org/6els PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6els RCSB], [http://www.ebi.ac.uk/pdbsum/6els PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6els ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6els" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Bijelic, A]] | |||
[[Category: Kampatsikas, I]] | [[Category: Kampatsikas, I]] | ||
[[Category: Pretzler, M]] | [[Category: Pretzler, M]] | ||
[[Category: Rompel, A]] | [[Category: Rompel, A]] | ||
[[Category: Latent form]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Polyphenol oxidase]] | |||
[[Category: Tyrosinase]] | |||
