View source for 6dhi


==Butelase 1: Auto-Catalytic Cleavage as an Evolutionary Constraint for Macrocyclizing Endopeptidases==
<StructureSection load='6dhi' size='340' side='right'caption='[[6dhi]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6dhi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clitoria_ternatea Clitoria ternatea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DHI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></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=6dhi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dhi OCA], [https://pdbe.org/6dhi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dhi RCSB], [https://www.ebi.ac.uk/pdbsum/6dhi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dhi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A060D9Z7_CLITE A0A060D9Z7_CLITE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plant asparaginyl endopeptidases (AEPs) are expressed as inactive zymogens that perform seed storage protein maturation upon cleavage dependent auto-activation in the low pH environment of storage vacuoles. AEPs have attracted attention for their macrocyclization reactions and have been classified as cleavage or ligation specialists. However, we have recently shown that the ability of AEPs to produce either cyclic or acyclic products can be altered by mutations to the active site region, and that several AEPs are capable of macrocyclization given favorable pH conditions. One AEP extracted from Clitoria ternatea seeds (butelase 1) is classified as a ligase rather than a protease, presenting an opportunity to test for loss of cleavage activity. Here, making recombinant butelase 1 and rescuing an Arabidopsis thaliana mutant lacking AEP, we show butelase 1 retains cleavage functions in vitro and in vivo. The in vivo rescue was incomplete, consistent with some trade-off for butelase 1 specialization toward macrocyclization. Its crystal structure showed an active site with only subtle differences from cleaving AEPs, suggesting the many differences in its peptide binding region are the source of its efficient macrocyclization. All considered, it seems either butelase 1 has not fully specialized or a requirement for auto-catalytic cleavage is an evolutionary constraint upon macrocyclizing AEPs. This article is protected by copyright. All rights reserved.

The macrocyclizing protease butelase 1 remains auto-catalytic and reveals the structural basis for ligase activity.,James AM, Haywood J, Leroux J, Ignasiak K, Elliott AG, Schmidberger JW, Fisher MF, Nonis SG, Fenske R, Bond CS, Mylne JS Plant J. 2019 Feb 21. doi: 10.1111/tpj.14293. PMID:30790358<ref>PMID:30790358</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6dhi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clitoria ternatea]]
[[Category: Large Structures]]
[[Category: Bond CS]]
[[Category: Haywood J]]