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6qtu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Arabidopsis WD40 domain in complex with a BBX transcription factor== | |
| - | + | <StructureSection load='6qtu' size='340' side='right'caption='[[6qtu]], [[Resolution|resolution]] 1.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6qtu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QTU FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RING-type_E3_ubiquitin_transferase RING-type E3 ubiquitin transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.27 2.3.2.27] </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=6qtu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qtu OCA], [http://pdbe.org/6qtu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qtu RCSB], [http://www.ebi.ac.uk/pdbsum/6qtu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qtu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/COP1_ARATH COP1_ARATH]] E3 ubiquitin-protein ligase that acts as a repressor of photomorphogenesis and as an activator of etiolation in darkness. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Represses photomorphogenesis in darkness by mediating ubiquitination and subsequent proteasomal degradation of light-induced transcription factors such as HY5, HYH and LAF1. Down-regulates MYB21, probably via ubiquitination process. Light stimuli abrogate the repression of photomorphogenesis, possibly due to its localization to the cytoplasm. Could play a role in switching between skotomorphogenetic and photomorphogenetic pathways.<ref>PMID:11967090</ref> <ref>PMID:12023303</ref> [[http://www.uniprot.org/uniprot/BBX24_ARATH BBX24_ARATH]] Acts as negative regulator of seedling photomorphogenesis and light-regulated inhibition of hypocotyl elongation (PubMed:17605755, PubMed:18540109, PubMed:21685177). BBX24/STO and BBX25/STH function as transcriptional corepressors of HY5 activity, leading to the down-regulation of BBX22 expression. BBX24/STO acts additively with BBX25/STH during de-etiolation and the hypocotyl shade avoidance response (PubMed:23624715). Functions as negative regulator of photomorphogenic UV-B responses by interacting with both COP1 and HY5 (PubMed:22410790). May act as a transcription factor in the salt-stress response (PubMed:12909688).<ref>PMID:12909688</ref> <ref>PMID:17605755</ref> <ref>PMID:18540109</ref> <ref>PMID:21685177</ref> <ref>PMID:22410790</ref> <ref>PMID:23624715</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: RING-type E3 ubiquitin transferase]] | ||
| + | [[Category: Hothorn, M]] | ||
[[Category: Lau, K]] | [[Category: Lau, K]] | ||
| - | [[Category: | + | [[Category: Complex]] |
| + | [[Category: Plant protein]] | ||
Revision as of 05:56, 10 July 2019
Crystal structure of Arabidopsis WD40 domain in complex with a BBX transcription factor
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