View source for 6ysa


==Crystal structure of Arabidopsis thaliana legumain isoform beta in zymogen state==
<StructureSection load='6ysa' size='340' side='right'caption='[[6ysa]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6ysa]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YSA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YSA 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]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6ysa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ysa OCA], [https://pdbe.org/6ysa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ysa RCSB], [https://www.ebi.ac.uk/pdbsum/6ysa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ysa ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VPEB_ARATH VPEB_ARATH] Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:12417707, PubMed:14688293).[UniProtKB:P49043]<ref>PMID:12417707</ref> <ref>PMID:14688293</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The vacuolar cysteine protease legumain plays important functions in seed maturation and plant programmed cell death. Because of their dual protease and ligase activity, plant legumains have become of particular biotechnological interest e.g. for the synthesis of cyclic peptides for drug design or for protein engineering. However, the molecular mechanisms behind their dual protease and ligase activities are still poorly understood, limiting their applications. Here we present the crystal structure of Arabidopsis thaliana legumain isoform beta (AtLEGbeta) in its zymogen state. Combining structural and biochemical experiments, we show for the first time that plant legumains encode distinct, isoform-specific activation mechanisms. While the autocatalytic activation of isoform gamma (AtLEGgamma) is controlled by the latency-conferring dimer state, the activation of the monomeric AtLEGbeta is concentration independent. Additionally, in AtLEGbeta the plant-characteristic two-chain intermediate state is stabilized by hydrophobic rather than ionic interactions as in AtLEGgamma, resulting in significantly different pH-stability profiles. The crystal structure of AtLEGbeta reveiled unrestricted non-prime substrate binding pockets, consistent with the broad substrate specificity as determined by degradomic assays. Further to its protease activity, we show that AtLEGbeta exhibits a true peptide ligase activity. While cleavage-dependent transpeptidase activity has been reported for other plant legumains, AtLEGbeta is the first example of a plant legumain capable of linking free termini. The discovery of these isoform specific differences will allow to identify and rationally design efficient ligases with application in biotechnology and drug development.

Structural and functional studies of Arabidopsis thaliana legumain beta reveal isoform specific mechanisms of activation and substrate recognition.,Dall E, Zauner FB, Soh WT, Demir F, Dahms SO, Cabrele C, Huesgen PF, Brandstetter H J Biol Chem. 2020 Jul 21. pii: RA120.014478. doi: 10.1074/jbc.RA120.014478. PMID:32719006<ref>PMID:32719006</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6ysa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Brandstetter H]]
[[Category: Dall E]]
[[Category: Zauner FB]]