6qtq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of an Arabidopsis WD40 domain in complex with photoreceptor== | |
| - | + | <StructureSection load='6qtq' size='340' side='right'caption='[[6qtq]], [[Resolution|resolution]] 1.30Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6qtq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QTQ 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=SO4:SULFATE+ION'>SO4</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=6qtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qtq OCA], [http://pdbe.org/6qtq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qtq RCSB], [http://www.ebi.ac.uk/pdbsum/6qtq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qtq 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/UVR8_ARATH UVR8_ARATH]] UV-B specific signaling component that acts as UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV-B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.<ref>PMID:16330762</ref> <ref>PMID:17720867</ref> <ref>PMID:18055587</ref> <ref>PMID:19165148</ref> <ref>PMID:19402876</ref> <ref>PMID:21041653</ref> <ref>PMID:21395889</ref> <ref>PMID:21454788</ref> <ref>PMID:22447155</ref> <ref>PMID:23161229</ref> <ref>PMID:23012433</ref> <ref>PMID:22988111</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 photoreceptor
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