6qtt - Revision history

OCA at 12:08, 24 January 2024

2024-01-24T12:08:33Z

←Older revision		Revision as of 12:08, 24 January 2024
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	<StructureSection load='6qtt' size='340' side='right'caption='[[6qtt]], [[Resolution\|resolution]] 1.51Å' scene=''>		<StructureSection load='6qtt' size='340' side='right'caption='[[6qtt]], [[Resolution\|resolution]] 1.51Å' scene=''>
	== Structural highlights ==		== 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>	+	<table><tr><td colspan='2'>[[6qtt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [https://proteopedia.org/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>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.51Å</td></tr>
-	<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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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'>[https://proteopedia.org/fgij/fg.htm?mol=6qtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qtt OCA], [https://pdbe.org/6qtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qtt RCSB], [https://www.ebi.ac.uk/pdbsum/6qtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qtt ProSAT]</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>		</table>
	== Function ==		== 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>	+	[https://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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Plants sense different parts of the sun's light spectrum using distinct photoreceptors, which signal through the E3 ubiquitin ligase COP1. Here, we analyze why many COP1-interacting transcription factors and photoreceptors harbor sequence-divergent Val-Pro (VP) motifs that bind COP1 with different binding affinities. Crystal structures of the VP motifs of the UV-B photoreceptor UVR8 and the transcription factor HY5 in complex with COP1, quantitative binding assays, and reverse genetic experiments together suggest that UVR8 and HY5 compete for COP1. Photoactivation of UVR8 leads to high-affinity cooperative binding of its VP motif and its photosensing core to COP1, preventing COP1 binding to its substrate HY5. UVR8-VP motif chimeras suggest that UV-B signaling specificity resides in the UVR8 photoreceptor core. Different COP1-VP peptide motif complexes highlight sequence fingerprints required for COP1 targeting. The blue-light photoreceptors CRY1 and CRY2 also compete with transcription factors for COP1 binding using similar VP motifs. Thus, our work reveals that different photoreceptors and their signaling components compete for COP1 via a conserved mechanism to control different light signaling cascades.
		+
		+	Plant photoreceptors and their signaling components compete for COP1 binding via VP peptide motifs.,Lau K, Podolec R, Chappuis R, Ulm R, Hothorn M EMBO J. 2019 Sep 16;38(18):e102140. doi: 10.15252/embj.2019102140. Epub 2019 Jul , 15. PMID:31304983<ref>PMID:31304983</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6qtt" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Arabidopsis thaliana]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: RING-type E3 ubiquitin transferase]]~~	+	[[Category: Hothorn M]]
-	[[Category: Hothorn, M]]	+	[[Category: Lau K]]
-	[[Category: Lau, K]]	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Plant protein~~]]	+

OCA at 05:55, 10 July 2019

2019-07-10T05:55:58Z

←Older revision		Revision as of 05:55, 10 July 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6qtt is ~~ON HOLD until Paper Publication~~	+	==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=''>
-	~~Authors~~: ~~Hothorn~~, M., ~~Lau~~, K.	+	== 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>
-	~~Description~~: ~~Crystal structure~~ of an ~~Arabidopsis WD40 domain~~ in ~~complex with~~ a transcription factor ~~homolog~~	+	</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: ~~Unreleased~~ Structures]]	+	<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: ~~Hothorn, M~~]]	+	[[Category: Complex]]
		+	[[Category: Plant protein]]

OCA: Protected "6qtt" [edit=sysop:move=sysop]

2019-03-06T05:54:06Z

Protected "6qtt" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:54, 6 March 2019

OCA: New page: '''Unreleased structure''' The entry 6qtt is ON HOLD until Paper Publication Authors: Hothorn, M., Lau, K. Description: Crystal structure of an Arabidopsis WD40 domain in complex with ...

2019-03-06T05:54:04Z

New page: '''Unreleased structure''' The entry 6qtt is ON HOLD until Paper Publication Authors: Hothorn, M., Lau, K. Description: Crystal structure of an Arabidopsis WD40 domain in complex with ...

New page

'''Unreleased structure'''

The entry 6qtt is ON HOLD until Paper Publication

Authors: Hothorn, M., Lau, K.

Description: Crystal structure of an Arabidopsis WD40 domain in complex with a transcription factor homolog
[[Category: Unreleased Structures]]
[[Category: Lau, K]]
[[Category: Hothorn, M]]