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| | ==Crystal structure of arabidopsis thaliana legumain isoform gamma in two-chain activation state== | | ==Crystal structure of arabidopsis thaliana legumain isoform gamma in two-chain activation state== |
| - | <StructureSection load='5nij' size='340' side='right' caption='[[5nij]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='5nij' size='340' side='right'caption='[[5nij]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nij]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NIJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nij]] is a 4 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=5NIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NIJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></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=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </span></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=5nij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nij OCA], [https://pdbe.org/5nij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nij RCSB], [https://www.ebi.ac.uk/pdbsum/5nij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nij ProSAT]</span></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=5nij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nij OCA], [http://pdbe.org/5nij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nij RCSB], [http://www.ebi.ac.uk/pdbsum/5nij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nij ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VPEG_ARATH VPEG_ARATH]] Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (PubMed:10417725). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:14688293).<ref>PMID:10417725</ref> <ref>PMID:14688293</ref> | + | [https://www.uniprot.org/uniprot/VPEG_ARATH VPEG_ARATH] Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (PubMed:10417725). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:14688293).<ref>PMID:10417725</ref> <ref>PMID:14688293</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Legumain]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Brandstetter, H]] | + | [[Category: Large Structures]] |
| - | [[Category: Dall, E]] | + | [[Category: Brandstetter H]] |
| - | [[Category: Zauner, F B]] | + | [[Category: Dall E]] |
| - | [[Category: Asparaginyl endopeptidase]] | + | [[Category: Zauner FB]] |
| - | [[Category: Cysteine protease]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Vacuolar processing enzyme]]
| + | |
| Structural highlights
Function
VPEG_ARATH Asparagine-specific endopeptidase involved in the processing of vacuolar seed protein precursors into the mature forms (PubMed:10417725). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:14688293).[1] [2]
Publication Abstract from PubMed
The vacuolar cysteine protease legumain can cleave and selectively rebuild peptide bonds, thereby vastly expanding the sequential repertoire of biomolecules. In this context, plant legumains have recently at-tracted particular interest. Furthermore, legumains have important roles in many physiological pro-cesses, including programmed cell death. Their efficient peptide bond ligase activity has gained tremen-dous interest in the design of cyclic peptides for drug design. However, the mechanistic understanding of these dual activities is incomplete and partly conflicting. Here we present the crystal structure of a plant legumain, Arabidopsis thaliana isoform-gamma (AtLEGgamma). Employing a conserved legumain fold, the plant legumain AtLEGgamma revealed unique mechanisms of auto-activation, including a plant-specific two-chain activation state, which remains conformationally stable at neutral pH, which is a prerequisite for full ligase activity and survival in different cell compartments. The charge distribution around the alpha6-helix mediates the pH-dependent dimerization and serves as a gatekeeper for the active site, thus regulating its protease and ligase activity.
Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation.,Zauner FB, Dall E, Regl C, Grassi L, Huber CG, Cabrele C, Brandstetter H Plant Cell. 2018 Feb 16. pii: tpc.17.00963. doi: 10.1105/tpc.17.00963. PMID:29453229[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kinoshita T, Yamada K, Hiraiwa N, Kondo M, Nishimura M, Hara-Nishimura I. Vacuolar processing enzyme is up-regulated in the lytic vacuoles of vegetative tissues during senescence and under various stressed conditions. Plant J. 1999 Jul;19(1):43-53. PMID:10417725
- ↑ Gruis D, Schulze J, Jung R. Storage protein accumulation in the absence of the vacuolar processing enzyme family of cysteine proteases. Plant Cell. 2004 Jan;16(1):270-90. doi: 10.1105/tpc.016378. Epub 2003 Dec 19. PMID:14688293 doi:http://dx.doi.org/10.1105/tpc.016378
- ↑ Zauner FB, Dall E, Regl C, Grassi L, Huber CG, Cabrele C, Brandstetter H. Crystal structure of plant legumain reveals a unique two-chain state with pH-dependent activity regulation. Plant Cell. 2018 Feb 16. pii: tpc.17.00963. doi: 10.1105/tpc.17.00963. PMID:29453229 doi:http://dx.doi.org/10.1105/tpc.17.00963
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