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| | <StructureSection load='5c7e' size='340' side='right'caption='[[5c7e]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5c7e' size='340' side='right'caption='[[5c7e]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c7e]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Orysa Orysa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C7E FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c7e]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C7E FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zhe|4zhe]], [[5c6q|5c6q]], [[5c6v|5c6v]], [[5c7f|5c7f]]</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=5c7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7e OCA], [https://pdbe.org/5c7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c7e RCSB], [https://www.ebi.ac.uk/pdbsum/5c7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c7e ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P0705D01.10-1, ASPR2, Os01g0254100, OsJ_01134 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4530 ORYSA])</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=5c7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c7e OCA], [http://pdbe.org/5c7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c7e RCSB], [http://www.ebi.ac.uk/pdbsum/5c7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c7e ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IAA10_ARATH IAA10_ARATH]] Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.<ref>PMID:12036262</ref> | + | [https://www.uniprot.org/uniprot/TPR1_ORYSJ TPR1_ORYSJ] Probable downstream regulator of strigolactones signaling.[UniProtKB:Q0J7U6] |
| | <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: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Orysa]] | + | [[Category: Oryza sativa]] |
| - | [[Category: Brunzelle, J S]] | + | [[Category: Brunzelle JS]] |
| - | [[Category: Gu, X]] | + | [[Category: Gu X]] |
| - | [[Category: Ke, J]] | + | [[Category: Ke J]] |
| - | [[Category: Ma, H]] | + | [[Category: Ma H]] |
| - | [[Category: Melcher, K]] | + | [[Category: Melcher K]] |
| - | [[Category: Xu, H E]] | + | [[Category: Xu HE]] |
| - | [[Category: Alpha-helical structure]]
| + | |
| - | [[Category: Plant development]]
| + | |
| - | [[Category: Plant transcriptional repression]]
| + | |
| - | [[Category: Tetrameric protein]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcriptional corepressor]]
| + | |
| Structural highlights
Function
TPR1_ORYSJ Probable downstream regulator of strigolactones signaling.[UniProtKB:Q0J7U6]
Publication Abstract from PubMed
TOPLESS (TPL) and TOPLESS-related (TPR) proteins comprise a conserved family of plant transcriptional corepressors that are related to Tup1, Groucho, and TLE (transducin-like enhancer of split) corepressors in yeast, insects, and mammals. In plants, TPL/TPR corepressors regulate development, stress responses, and hormone signaling through interaction with small ethylene response factor-associated amphiphilic repression (EAR) motifs found in diverse transcriptional repressors. How EAR motifs can interact with TPL/TPR proteins is unknown. We confirm the amino-terminal domain of the TPL family of corepressors, which we term TOPLESS domain (TPD), as the EAR motif-binding domain. To understand the structural basis of this interaction, we determined the crystal structures of the TPD of rice (Os) TPR2 in apo (apo protein) state and in complexes with the EAR motifs from Arabidopsis NINJA (novel interactor of JAZ), IAA1 (auxin-responsive protein 1), and IAA10, key transcriptional repressors involved in jasmonate and auxin signaling. The OsTPR2 TPD adopts a new fold of nine helices, followed by a zinc finger, which are arranged into a disc-like tetramer. The EAR motifs in the three different complexes adopt a similar extended conformation with the hydrophobic residues fitting into the same surface groove of each OsTPR2 monomer. Sequence alignments and structure-based mutagenesis indicate that this mode of corepressor binding is highly conserved in a large set of transcriptional repressors, thus providing a general mechanism for gene repression mediated by the TPL family of corepressors.
Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors.,Ke J, Ma H, Gu X, Thelen A, Brunzelle JS, Li J, Xu HE, Melcher K Sci Adv. 2015 Jul 24;1(6):e1500107. eCollection 2015 Jul. PMID:26601214[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ke J, Ma H, Gu X, Thelen A, Brunzelle JS, Li J, Xu HE, Melcher K. Structural basis for recognition of diverse transcriptional repressors by the TOPLESS family of corepressors. Sci Adv. 2015 Jul 24;1(6):e1500107. eCollection 2015 Jul. PMID:26601214 doi:http://dx.doi.org/10.1126/sciadv.1500107
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