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2rt9

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Revision as of 13:45, 11 August 2016

Solution structure of a regulatory domain of meiosis inhibitor

Structural highlights

2rt9 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FBX43_MOUSE] Required to establish and maintain the arrest of oocytes at the second meiotic metaphase until fertilization. Probably acts by inhibiting the anaphase-promoting complex/cyclosome (APC/C) ubiquitin ligase. Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation.

Publication Abstract from PubMed

Anaphase-promoting complex or cyclosome (APC/C) is a multisubunit ubiquitin ligase E3 that targets cell-cycle regulators. Cdc20 is required for full activation of APC/C in M phase, and mediates substrate recognition. In vertebrates, Emi2/Erp1/FBXO43 inhibits APC/C-Cdc20, and functions as a cytostatic factor that causes long-term M phase arrest of mature oocytes. In this study, we found that a fragment corresponding to the zinc-binding region (ZBR) domain of Emi2 inhibits cell-cycle progression, and impairs the association of Cdc20 with the APC/C core complex in HEK293T cells. Furthermore, we revealed that the ZBR fragment of Emi2 inhibits in vitro ubiquitin chain elongation catalyzed by the APC/C cullin-RING ligase module, the ANAPC2-ANAPC11 subcomplex, in combination with the ubiquitin chain-initiating E2, E2C/UBE2C/UbcH10. Structural analyses revealed that the Emi2 ZBR domain uses different faces for the two mechanisms. Thus, the double-faced ZBR domain of Emi2 antagonizes the APC/C function by inhibiting both the binding with the coactivator Cdc20 and ubiquitylation mediated by the cullin-RING ligase module and E2C. In addition, the tail region between the ZBR domain and the C-terminal RL residues [the post-ZBR (PZ) region] interacts with the cullin subunit, ANAPC2. In the case of the ZBR fragment of the somatic paralogue of Emi2, Emi1/FBXO5, these inhibitory activities against cell division and ubiquitylation were not observed. Finally, we identified two sets of key residues in the Emi2 ZBR domain that selectively exert each of the dual Emi2-specific modes of APC/C inhibition, by their mutation in the Emi2 ZBR domain and their transplantation into the Emi1 ZBR domain.

The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation.,Shoji S, Muto Y, Ikeda M, He F, Tsuda K, Ohsawa N, Akasaka R, Terada T, Wakiyama M, Shirouzu M, Yokoyama S FEBS Open Bio. 2014 Jul 5;4:689-703. doi: 10.1016/j.fob.2014.06.010. eCollection , 2014. PMID:25161877^[1]

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

References

↑ Shoji S, Muto Y, Ikeda M, He F, Tsuda K, Ohsawa N, Akasaka R, Terada T, Wakiyama M, Shirouzu M, Yokoyama S. The zinc-binding region (ZBR) fragment of Emi2 can inhibit APC/C by targeting its association with the coactivator Cdc20 and UBE2C-mediated ubiquitylation. FEBS Open Bio. 2014 Jul 5;4:689-703. doi: 10.1016/j.fob.2014.06.010. eCollection , 2014. PMID:25161877 doi:http://dx.doi.org/10.1016/j.fob.2014.06.010

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/2rt9"

@@ Line 1: / Line 1: @@
 ==Solution structure of a regulatory domain of meiosis inhibitor==
 <StructureSection load='2rt9' size='340' side='right' caption='[[2rt9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[2rt9]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RT9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2rt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt9 PDBsum]</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=2rt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rt9 OCA], [http://pdbe.org/2rt9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rt9 RCSB], [http://www.ebi.ac.uk/pdbsum/2rt9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rt9 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2rt9" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2rt9

From Proteopedia

Revision as of 13:45, 11 August 2016

Solution structure of a regulatory domain of meiosis inhibitor

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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