Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Mechanism of Ψ-Pro/C-degron recognition by the CRL2 ubiquitin ligase.
Journal, issue, pages	Nat Commun, Vol. 15, Issue 1, Page 3558, Year 2024
Publish date	Apr 26, 2024
Authors	Xinyan Chen / Anat Raiff / Shanshan Li / Qiong Guo / Jiahai Zhang / Hualin Zhou / Richard T Timms / Xuebiao Yao / Stephen J Elledge / Itay Koren / Kaiming Zhang / Chao Xu /
PubMed Abstract	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- ...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 bound to different C-degrons, we elucidate the dimeric assembly of the complex. Furthermore, we reveal distinct dimerization states of unmodified and neddylated CRL2 to uncover the NEDD8-mediated activation mechanism of CRL2. 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-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.
External links	Nat Commun / PubMed:38670995 / PubMed Central
Methods	EM (single particle)
Resolution	3.27 - 4.09 Å
Structure data	37736 8wqa EMDB-37736, PDB-8wqa: Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89 (conformation 1) Method: EM (single particle) / Resolution: 3.39 Å 37737 8wqb EMDB-37737, PDB-8wqb: Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89 (conformation 2) Method: EM (single particle) / Resolution: 3.37 Å 37739 8wqc EMDB-37739, PDB-8wqc: cryo-EM structure of neddylated CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CDK5R1 Method: EM (single particle) / Resolution: 3.54 Å 37740 8wqd EMDB-37740, PDB-8wqd: Local refinement of FEM1B bound with the C-degron of CCC89 Method: EM (single particle) / Resolution: 3.55 Å 37742 8wqe EMDB-37742, PDB-8wqe: Cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1 (conformation 1) Method: EM (single particle) / Resolution: 3.38 Å 37743 8wqf EMDB-37743, PDB-8wqf: cryo-EM structure of CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CUX1 (conformation 2) Method: EM (single particle) / Resolution: 3.27 Å 37744 8wqg EMDB-37744, PDB-8wqg: cryo-EM structure of neddylated CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89 (conformation 1) Method: EM (single particle) / Resolution: 4.09 Å 37745 8wqh EMDB-37745, PDB-8wqh: cryo-EM structure of neddylated CUL2-RBX1-ELOB-ELOC-FEM1B bound with the C-degron of CCDC89 (conformation 2) Method: EM (single particle) / Resolution: 3.44 Å 37746 8wqi EMDB-37746, PDB-8wqi: Local refinement of FEM1B bound with the C-degron of CUX1 Method: EM (single particle) / Resolution: 3.5 Å
Chemicals	ChemComp-ZN: Unknown entry
Source	homo sapiens (human)
Keywords	LIGASE / E3 ubiquitin ligase / Pro/C-degron / PROTEIN BINDING