5svg
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Structure and kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis== | |
- | + | <StructureSection load='5svg' size='340' side='right' caption='[[5svg]], [[Resolution|resolution]] 2.50Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[5svg]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SVG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SVG FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |
- | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5svu|5svu]], [[5svv|5svv]], [[5svw|5svw]]</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=5svg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5svg OCA], [http://pdbe.org/5svg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5svg RCSB], [http://www.ebi.ac.uk/pdbsum/5svg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5svg ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/ADO1_ARATH ADO1_ARATH]] Component of an E3 ubiquitin ligase complex that plays a central role in blue light-dependent circadian cycles. Acts as a blue light photoreceptor, due to the presence of FMN, that mediates light-regulated protein degradation of critical clock components by targeting them to the proteasome complex. The SCF(ADO1) E3 ubiquitin ligase complex is involved in the regulation of circadian clock-dependent processes including the transition to flowering time, hypocotyl elongation, cotyledons and leaf movement rhythms. APRR1/TOC1 and APRR5, but not 'GIGANTEA', are proteolytic substrates of this ubiquitin ligase complex. Blue light enhances cooperative stabilization of 'GIGANTEA' and ADO1/ZTL, leading to amplification and sharpening of the expression profile of APRR1/TOC1. ADO1/ZTL interacts with ADO3, preventing the interaction of ADO3 with CDF1.<ref>PMID:10847686</ref> <ref>PMID:10847687</ref> <ref>PMID:10998191</ref> <ref>PMID:11260718</ref> <ref>PMID:14973171</ref> <ref>PMID:15447654</ref> <ref>PMID:16428597</ref> <ref>PMID:17704763</ref> <ref>PMID:21518052</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Pudasaini, A]] | ||
+ | [[Category: Zoltowski, B]] | ||
+ | [[Category: Circadian clock protein]] | ||
+ | [[Category: Kinetic]] | ||
+ | [[Category: Lov]] | ||
+ | [[Category: Pas domain]] | ||
+ | [[Category: Photoreceptor]] |
Revision as of 19:17, 11 March 2017
Structure and kinetics of the LOV domain of ZEITLUPE determine its circadian function in Arabidopsis
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