8wqg

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Current revision (10:03, 9 October 2024) (edit) (undo)
 
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8wqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wqg OCA], [https://pdbe.org/8wqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wqg RCSB], [https://www.ebi.ac.uk/pdbsum/8wqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wqg ProSAT]</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=8wqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wqg OCA], [https://pdbe.org/8wqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wqg RCSB], [https://www.ebi.ac.uk/pdbsum/8wqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wqg ProSAT]</span></td></tr>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/ELOB_HUMAN ELOB_HUMAN] SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex).<ref>PMID:7638163</ref> <ref>PMID:15590694</ref> The elongin BC complex seems to be involved as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes, including the von Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-box motifs it seems to link target recruitment subunits, like VHL and members of the SOCS box family, to Cullin/RBX1 modules that activate E2 ubiquitination enzymes.<ref>PMID:7638163</ref> <ref>PMID:15590694</ref>
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== Publication Abstract from PubMed ==
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The E3 ligase-degron interaction determines the specificity of the ubiquitin‒proteasome system. We recently discovered that FEM1B, a substrate receptor of Cullin 2-RING ligase (CRL2), recognizes C-degrons containing a C-terminal proline. By solving several cryo-EM structures of CRL2(FEM1B) bound to different C-degrons, we elucidate the dimeric assembly of the complex. Furthermore, we reveal distinct dimerization states of unmodified and neddylated CRL2(FEM1B) to uncover the NEDD8-mediated activation mechanism of CRL2(FEM1B). Our research also indicates that, FEM1B utilizes a bipartite mechanism to recognize both the C-terminal proline and an upstream aromatic residue within the substrate. These structural findings, complemented by in vitro ubiquitination and in vivo cell-based assays, demonstrate that CRL2(FEM1B)-mediated polyubiquitination and subsequent protein turnover depend on both FEM1B-degron interactions and the dimerization state of the E3 ligase complex. Overall, this study deepens our molecular understanding of how Cullin-RING E3 ligase substrate selection mediates protein turnover.
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Mechanism of Psi-Pro/C-degron recognition by the CRL2(FEM1B) ubiquitin ligase.,Chen X, Raiff A, Li S, Guo Q, Zhang J, Zhou H, Timms RT, Yao X, Elledge SJ, Koren I, Zhang K, Xu C Nat Commun. 2024 Apr 26;15(1):3558. doi: 10.1038/s41467-024-47890-5. PMID:38670995<ref>PMID:38670995</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 8wqg" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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Current revision

cryo-EM structure of neddylated CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89 (conformation 1)

PDB ID 8wqg

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