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| | ==Crystal structure of plant protease Deg2== | | ==Crystal structure of plant protease Deg2== |
| - | <StructureSection load='4fln' size='340' side='right' caption='[[4fln]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4fln' size='340' side='right'caption='[[4fln]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4fln]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath] and [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FLN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FLN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4fln]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FLN FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | + | </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=4fln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fln OCA], [https://pdbe.org/4fln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fln RCSB], [https://www.ebi.ac.uk/pdbsum/4fln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fln ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEGP2, At2g47940, F17A22.33, T9J23.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
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| - | <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=4fln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fln OCA], [http://pdbe.org/4fln PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fln RCSB], [http://www.ebi.ac.uk/pdbsum/4fln PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fln ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DEGP2_ARATH DEGP2_ARATH]] Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.<ref>PMID:11179216</ref> | + | [https://www.uniprot.org/uniprot/DEGP2_ARATH DEGP2_ARATH] Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.<ref>PMID:11179216</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: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Miscellaneous nucleic acid]] | + | [[Category: Large Structures]] |
| - | [[Category: Gao, F]] | + | [[Category: Unidentified]] |
| - | [[Category: Gong, W]] | + | [[Category: Gao F]] |
| - | [[Category: Liu, L]] | + | [[Category: Gong W]] |
| - | [[Category: Sun, R]] | + | [[Category: Liu L]] |
| - | [[Category: Deg]]
| + | [[Category: Sun R]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Pdz]]
| + | |
| - | [[Category: Protease]]
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| Structural highlights
Function
DEGP2_ARATH Serine protease that performs the primary cleavage of the photodamaged D1 protein in plant photosystem II.[1]
Publication Abstract from PubMed
Eukaryotic organelles have developed elaborate protein quality control systems to ensure their normal activity, among which Deg/HtrA proteases play an essential role. Plant Deg2 protease is a homologue of prokaryotic DegQ/DegP proteases and located in the chloroplast stroma, where its proteolytic activity is required to maintain the efficiency of photosynthetic machinery during stress. Here, we demonstrate that Deg2 exhibits dual protease-chaperone activities, and present the hexameric structure of Deg2 complexed with co-purified peptides. The structure shows that Deg2 contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of Deg2. We discover a conserved internal ligand for PDZ2 that mediates hexamer formation, thus locks the protease in the resting state. These findings provide insight into the diverse modes of PDZ-mediated regulation of Deg proteases.
Crystal structure of Arabidopsis Deg2 reveals an internal PDZ ligand locking the hexameric resting state.,Sun R, Fan H, Gao F, Lin Y, Zhang L, Gong W, Liu L J Biol Chem. 2012 Sep 7. PMID:22961982[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Haussuhl K, Andersson B, Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 2001 Feb 15;20(4):713-22. PMID:11179216 doi:http://dx.doi.org/10.1093/emboj/20.4.713
- ↑ Sun R, Fan H, Gao F, Lin Y, Zhang L, Gong W, Liu L. Crystal structure of Arabidopsis Deg2 reveals an internal PDZ ligand locking the hexameric resting state. J Biol Chem. 2012 Sep 7. PMID:22961982 doi:http://dx.doi.org/10.1074/jbc.M112.394585
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