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| | <StructureSection load='7obe' size='340' side='right'caption='[[7obe]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='7obe' size='340' side='right'caption='[[7obe]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7obe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5obl 5obl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OBE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7obe]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5obl 5obl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OBE FirstGlance]. <br> |
| - | </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=MN:MANGANESE+(II)+ION'>MN</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]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAPP5, PP5, At2g42810, F7D19.19 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </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=7obe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7obe OCA], [https://pdbe.org/7obe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7obe RCSB], [https://www.ebi.ac.uk/pdbsum/7obe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7obe ProSAT]</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=7obe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7obe OCA], [https://pdbe.org/7obe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7obe RCSB], [https://www.ebi.ac.uk/pdbsum/7obe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7obe ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PPP5_ARATH PPP5_ARATH]] Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses, probably by enhancing their stability and their binding affinity for light signal transducers such as NDPK2. Can use para-nitrophenylphosphate (pNPP) as substrate.<ref>PMID:15707897</ref>
| + | [https://www.uniprot.org/uniprot/PPP5_ARATH PPP5_ARATH] Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses, probably by enhancing their stability and their binding affinity for light signal transducers such as NDPK2. Can use para-nitrophenylphosphate (pNPP) as substrate.<ref>PMID:15707897</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: Large Structures]] | |
| - | [[Category: Phosphoprotein phosphatase]] | |
| - | [[Category: Essen, L O]] | |
| - | [[Category: Horsten, S von]] | |
| | [[Category: Arabidopsis thaliana]] | | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Hydrolase]] | + | [[Category: Large Structures]] |
| - | [[Category: Phosphatase]] | + | [[Category: Essen L-O]] |
| - | [[Category: Pp5]] | + | [[Category: Von Horsten S]] |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
PPP5_ARATH Isoform 2 dephosphorylates phosphorylated phytochromes, with a preference toward Pfr forms, and enhances phytochrome-mediated photoresponses, probably by enhancing their stability and their binding affinity for light signal transducers such as NDPK2. Can use para-nitrophenylphosphate (pNPP) as substrate.[1]
Publication Abstract from PubMed
Phytochrome activity is not only controlled by light but also by post-translational modifications, e. g. phosphorylation. One of the phosphatases responsible for plant phytochrome dephosphorylation and thereby increased activity is the phytochrome-associated protein phosphatase 5 (PAPP5). We show that PAPP5 recognizes phospho-site mimicking mutants of phytochrome B, when being activated by arachidonic acid (AA). Addition of AA to PAPP5 decreases the alpha-helical content as tracked by CD-spectroscopy. These changes correspond to conformational changes of the regulatory tetratricopeptide repeats (TPR) region as shown by mapping data from hydrogen deuterium exchange mass spectrometry onto a 3.0 A crystal structure of PAPP5. Surprisingly, parts of the linker between the TPR and PP2A domains and of the so-called C-terminal inhibitory motif exhibit reduced deuterium uptake upon AA-binding. Molecular dynamics analyses of PAPP5 complexed to a phyB phosphopeptide show that this C-terminal motif remains associated with the TPR region in the substrate bound state, suggesting that this motif merely serves for restricting the orientations of the TPR region relative to the catalytic PP2A domain. Given the high similarity to mammalian PP5 these data from a plant ortholog show that the activation mode of these PPP-type protein phosphatases is highly conserved.
Conformational Change of Tetratricopeptide Repeats Region Triggers Activation of Phytochrome-Associated Protein Phosphatase 5.,von Horsten S, Essen LO Front Plant Sci. 2021 Oct 14;12:733069. doi: 10.3389/fpls.2021.733069., eCollection 2021. PMID:34721460[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ryu JS, Kim JI, Kunkel T, Kim BC, Cho DS, Hong SH, Kim SH, Fernandez AP, Kim Y, Alonso JM, Ecker JR, Nagy F, Lim PO, Song PS, Schafer E, Nam HG. Phytochrome-specific type 5 phosphatase controls light signal flux by enhancing phytochrome stability and affinity for a signal transducer. Cell. 2005 Feb 11;120(3):395-406. PMID:15707897 doi:http://dx.doi.org/10.1016/j.cell.2004.12.019
- ↑ von Horsten S, Essen LO. Conformational Change of Tetratricopeptide Repeats Region Triggers Activation of Phytochrome-Associated Protein Phosphatase 5. Front Plant Sci. 2021 Oct 14;12:733069. doi: 10.3389/fpls.2021.733069., eCollection 2021. PMID:34721460 doi:http://dx.doi.org/10.3389/fpls.2021.733069
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