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| | <StructureSection load='4y0c' size='340' side='right'caption='[[4y0c]], [[Resolution|resolution]] 1.99Å' scene=''> | | <StructureSection load='4y0c' size='340' side='right'caption='[[4y0c]], [[Resolution|resolution]] 1.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y0c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y0c]] is a 2 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=4Y0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4y0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0c OCA], [https://pdbe.org/4y0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0c RCSB], [https://www.ebi.ac.uk/pdbsum/4y0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0c ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0b|4y0b]]</td></tr>
| + | |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At4g12060, F16J13.130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4y0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0c OCA], [http://pdbe.org/4y0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0c RCSB], [http://www.ebi.ac.uk/pdbsum/4y0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/CLPT2_ARATH CLPT2_ARATH] Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed:21266658, PubMed:25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed:21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed:21266658). CLPT2 and CLPT1 are partially redundant (PubMed:25921872).<ref>PMID:21266658</ref> <ref>PMID:25921872</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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kimber, M S]] | + | [[Category: Kimber MS]] |
| - | [[Category: Schultz, L]] | + | [[Category: Schultz L]] |
| - | [[Category: Alpha helical bundle]]
| + | |
| - | [[Category: Caseinolytic protease]]
| + | |
| - | [[Category: N-domain]]
| + | |
| - | [[Category: Plastid]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Function
CLPT2_ARATH Accessory protein regulating the assembly of the plastidial Clp protease system (PubMed:21266658, PubMed:25921872). CLPT1 first binds to the heptameric P-ring containing the CLP3-6 subunits followed by CLPT2, and only then does the P-ring combine with the R-ring composed of the clpP1 and CLPR1-4 subunits (PubMed:21266658). Once the core complex is fully assembled, it then associates to the CLPC chaperone partner to form the functional protease (PubMed:21266658). CLPT2 and CLPT1 are partially redundant (PubMed:25921872).[1] [2]
Publication Abstract from PubMed
Plastid ClpT1 and ClpT2 are plant-specific proteins that associate with the ClpPR protease. However, their physiological significance and structures are not understood. Arabidopsis thaliana loss-of-function single clpt1 and clpt2 mutants showed no visible phenotypes, whereas clpt1 clpt2 double mutants showed delayed development, reduced plant growth, and virescent, serrated leaves but were viable and produced seed. The clpt1 and clpt1 clpt2 mutants showed partial destabilization of the ClpPR complex, whereas clpt2 null mutants showed only marginal destabilization. Comparative proteomics of clpt1 clpt2 plants showed a proteostasis phenotype similar to viable mutants in ClpPR core subunits, indicating reduced Clp protease capacity. In vivo and in vitro assays showed that ClpT1 and ClpT2 can independently interact with the single ClpP ring and ClpPR core, but not with the single ClpR ring. We determined ClpT1 and ClpT2 structures (2.4- and 2.0-A resolution) and detailed the similarities to the N-domains of bacterial ClpA/C chaperones. The ClpT structures suggested a conserved MYFF motif for interaction with the ClpPR core near the interface between the P- and R-rings. In vivo complementation showed that ClpT function and ClpPR core stabilization require the MYFF motif. Several models are presented that may explain how ClpT1,2 contribute to ClpPR protease activity.
Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts.,Kim J, Kimber MS, Nishimura K, Friso G, Schultz L, Ponnala L, van Wijk KJ Plant Cell. 2015 Apr 28. pii: tpc.15.00106. PMID:25921872[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sjögren LL, Clarke AK. Assembly of the chloroplast ATP-dependent Clp protease in Arabidopsis is regulated by the ClpT accessory proteins. Plant Cell. 2011 Jan;23(1):322-32. PMID:21266658 doi:10.1105/tpc.110.082321
- ↑ Kim J, Kimber MS, Nishimura K, Friso G, Schultz L, Ponnala L, van Wijk KJ. Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts. Plant Cell. 2015 Apr 28. pii: tpc.15.00106. PMID:25921872 doi:http://dx.doi.org/10.1105/tpc.15.00106
- ↑ Kim J, Kimber MS, Nishimura K, Friso G, Schultz L, Ponnala L, van Wijk KJ. Structures, Functions, and Interactions of ClpT1 and ClpT2 in the Clp Protease System of Arabidopsis Chloroplasts. Plant Cell. 2015 Apr 28. pii: tpc.15.00106. PMID:25921872 doi:http://dx.doi.org/10.1105/tpc.15.00106
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