6elt

<table><tr><td colspan='2'>[[6elt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apple Apple]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ELT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ELT FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6els|6els]]</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=6elt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6elt OCA], [http://pdbe.org/6elt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6elt RCSB], [http://www.ebi.ac.uk/pdbsum/6elt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6elt ProSAT]</span></td></tr>

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== 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.

 

== References ==

[[Category: Apple]]

[[Category: Bijelic, A]]

[[Category: Kampatsikas, I]]

[[Category: Pretzler, M]]

[[Category: Rompel, A]]

[[Category: Tyrosinase]]