5igo

From Proteopedia

(Difference between revisions)

Revision as of 12:45, 16 November 2017

WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1

Structural highlights

5igo is a 8 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	COP1, At2g32950, T21L14.11 (ARATH)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] [TRIB1_HUMAN] Interacts with MAPK kinases and regulates activation of MAP kinases. May not display kinase activity.^[3] ^[4]

Publication Abstract from PubMed

COP1 proteins are E3 ubiquitin ligases that regulate phototropism in plants and target transcription factors for degradation in mammals. The substrate-binding region of COP1 resides within a WD40-repeat domain that also binds to Trib proteins, which are adaptors for C/EBPalpha degradation. Here we report structures of the human COP1 WD40 domain in isolation, and complexes of the human and Arabidopsis thaliana COP1 WD40 domains with the binding motif of Trib1. The human and Arabidopsis WD40 domains are seven-bladed beta propellers with an inserted loop on the bottom face of the first blade. The Trib1 peptide binds in an extended conformation to a highly conserved surface on the top face of the beta propeller, indicating a general mode for recognition of peptide motifs by COP1. Together, these studies identify the structural basis and key interactions for motif recognition by COP1, and hint at how Trib1 autoinhibition is overcome to target C/EBPalpha for degradation.

Structural Basis for Substrate Selectivity of the E3 Ligase COP1.,Uljon S, Xu X, Durzynska I, Stein S, Adelmant G, Marto JA, Pear WS, Blacklow SC Structure. 2016 May 3;24(5):687-96. doi: 10.1016/j.str.2016.03.002. Epub 2016 Mar, 31. PMID:27041596^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Shin B, Choi G, Yi H, Yang S, Cho I, Kim J, Lee S, Paek NC, Kim JH, Song PS, Choi G. AtMYB21, a gene encoding a flower-specific transcription factor, is regulated by COP1. Plant J. 2002 Apr;30(1):23-32. PMID:11967090
↑ Holm M, Ma LG, Qu LJ, Deng XW. Two interacting bZIP proteins are direct targets of COP1-mediated control of light-dependent gene expression in Arabidopsis. Genes Dev. 2002 May 15;16(10):1247-59. PMID:12023303 doi:http://dx.doi.org/10.1101/gad.969702
↑ Kiss-Toth E, Bagstaff SM, Sung HY, Jozsa V, Dempsey C, Caunt JC, Oxley KM, Wyllie DH, Polgar T, Harte M, O'neill LA, Qwarnstrom EE, Dower SK. Human tribbles, a protein family controlling mitogen-activated protein kinase cascades. J Biol Chem. 2004 Oct 8;279(41):42703-8. Epub 2004 Aug 6. PMID:15299019 doi:http://dx.doi.org/10.1074/jbc.M407732200
↑ Kiss-Toth E, Bagstaff SM, Sung HY, Jozsa V, Dempsey C, Caunt JC, Oxley KM, Wyllie DH, Polgar T, Harte M, O'neill LA, Qwarnstrom EE, Dower SK. Human tribbles, a protein family controlling mitogen-activated protein kinase cascades. J Biol Chem. 2004 Oct 8;279(41):42703-8. Epub 2004 Aug 6. PMID:15299019 doi:http://dx.doi.org/10.1074/jbc.M407732200
↑ Uljon S, Xu X, Durzynska I, Stein S, Adelmant G, Marto JA, Pear WS, Blacklow SC. Structural Basis for Substrate Selectivity of the E3 Ligase COP1. Structure. 2016 May 3;24(5):687-96. doi: 10.1016/j.str.2016.03.002. Epub 2016 Mar, 31. PMID:27041596 doi:http://dx.doi.org/10.1016/j.str.2016.03.002

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5igo"

Categories: Arath | Blacklow, S C | Uljon, S | Hydrolase-peptide complex | Wd40 domain e3 ligase

@@ Line 3: / Line 3: @@
 <StructureSection load='5igo' size='340' side='right' caption='[[5igo]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5igo]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IGO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5igo]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IGO FirstGlance]. <br>
-</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=5igo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5igo OCA], [http://pdbe.org/5igo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5igo RCSB], [http://www.ebi.ac.uk/pdbsum/5igo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5igo ProSAT]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COP1, At2g32950, T21L14.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=5igo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5igo OCA], [http://pdbe.org/5igo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5igo RCSB], [http://www.ebi.ac.uk/pdbsum/5igo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5igo ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Arath]]
 [[Category: Blacklow, S C]]
 [[Category: Uljon, S]]
 [[Category: Hydrolase-peptide complex]]
 [[Category: Wd40 domain e3 ligase]]

5igo

From Proteopedia

Revision as of 12:45, 16 November 2017

WD40 domain of Arabidopsis thaliana E3 Ubiquitin Ligase COP1 in complex with peptide from Trib1

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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