View source for 5a24


==Crystal structure of Dionain-1, the major endopeptidase in the Venus flytrap digestive juice==
<StructureSection load='5a24' size='340' side='right'caption='[[5a24]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5a24]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dionaea_muscipula Dionaea muscipula]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A24 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=5a24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a24 OCA], [https://pdbe.org/5a24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a24 RCSB], [https://www.ebi.ac.uk/pdbsum/5a24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a24 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0E3GLN3_DIOMU A0A0E3GLN3_DIOMU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Carnivorous plants primarily use aspartic proteases during digestion of captured prey. In contrast, the major endopeptidases in the digestive fluid of the Venus flytrap (Dionaea muscipula) are cysteine proteases (dionain-1 to -4). Here, we present the crystal structure of mature dionain-1 in covalent complex with inhibitor E-64 at 1.5 A resolution. The enzyme exhibits an overall protein fold reminiscent of other plant cysteine proteases. The inactive glycosylated pro-form undergoes autoprocessing and self-activation, optimally at the physiologically relevant pH value of 3.6, at which the protective effect of the pro-domain is lost. The mature enzyme was able to efficiently degrade a Drosophila fly protein extract at pH 4 showing high activity against the abundant Lys- and Arg-rich protein, myosin. The substrate specificity of dionain-1 was largely similar to that of papain with preference for hydrophobic and aliphatic residues in subsite S2 and for positively charged residues in S1. A tentative structure of the pro-domain was obtained by homology modeling and suggested that a pro-peptide Lys residue intrudes the S2 pocket which is more spacious than in papain. This study provides the first analysis of a cysteine protease from the digestive fluid of a carnivorous plant and confirms the close relationship between carnivorous action and plant defense mechanisms.

Enzymatic and structural characterization of the major endopeptidase in the Venus flytrap digestion fluid.,Risor MW, Thomsen LR, Sanggaard KW, Nielsen TA, Thogersen IB, Lukassen MV, Rossen L, Garcia-Ferrer I, Guevara T, Scavenius C, Meinjohanns E, Gomis-Ruth FX, Enghild JJ J Biol Chem. 2015 Dec 1. pii: jbc.M115.672550. PMID:26627834<ref>PMID:26627834</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5a24" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dionaea muscipula]]
[[Category: Large Structures]]
[[Category: Enghild JJ]]
[[Category: Garcia-Ferrer I]]
[[Category: Gomis-Ruth FX]]
[[Category: Guevara T]]
[[Category: Lukassen MV]]
[[Category: Meinjohanns E]]
[[Category: Nielsen NC]]
[[Category: Nielsen TA]]
[[Category: Risor MW]]
[[Category: Rossen L]]
[[Category: Sanggaard KW]]
[[Category: Thogersen IB]]
[[Category: Thomsen LR]]