6qtt
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of an Arabidopsis WD40 domain in complex with a transcription factor homolog== | |
| - | + | <StructureSection load='6qtt' size='340' side='right'caption='[[6qtt]], [[Resolution|resolution]] 1.51Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6qtt]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QTT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QTT 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=6qtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qtt OCA], [http://pdbe.org/6qtt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qtt RCSB], [http://www.ebi.ac.uk/pdbsum/6qtt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qtt 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/HYH_ARATH HYH_ARATH]] Transcription factor that promotes photomorphogenesis in light. Acts downstream of the light receptor network and directly affects transcription of light-induced genes. Specifically involved in the blue light specific pathway, suggesting that it participates in transmission of cryptochromes (CRY1 and CRY2) signals to downstream responses. In darkness, its degradation prevents the activation of light-induced genes.<ref>PMID:12023303</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 05:55, 10 July 2019
Crystal structure of an Arabidopsis WD40 domain in complex with a transcription factor homolog
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