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	Ubiquitin ligation to F-box protein targets by SCF-RBR E3-E3 super-assembly.
Journal, issue, pages	Nature, Vol. 590, Issue 7847, Page 671-676, Year 2021
Publish date	Feb 3, 2021
Authors	Daniel Horn-Ghetko / David T Krist / J Rajan Prabu / Kheewoong Baek / Monique P C Mulder / Maren Klügel / Daniel C Scott / Huib Ovaa / Gary Kleiger / Brenda A Schulman /
PubMed Abstract	E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates. However, rather ...E3 ligases are typically classified by hallmark domains such as RING and RBR, which are thought to specify unique catalytic mechanisms of ubiquitin transfer to recruited substrates. However, rather than functioning individually, many neddylated cullin-RING E3 ligases (CRLs) and RBR-type E3 ligases in the ARIH family-which together account for nearly half of all ubiquitin ligases in humans-form E3-E3 super-assemblies. Here, by studying CRLs in the SKP1-CUL1-F-box (SCF) family, we show how neddylated SCF ligases and ARIH1 (an RBR-type E3 ligase) co-evolved to ubiquitylate diverse substrates presented on various F-box proteins. We developed activity-based chemical probes that enabled cryo-electron microscopy visualization of steps in E3-E3 ubiquitylation, initiating with ubiquitin linked to the E2 enzyme UBE2L3, then transferred to the catalytic cysteine of ARIH1, and culminating in ubiquitin linkage to a substrate bound to the SCF E3 ligase. The E3-E3 mechanism places the ubiquitin-linked active site of ARIH1 adjacent to substrates bound to F-box proteins (for example, substrates with folded structures or limited length) that are incompatible with previously described conventional RING E3-only mechanisms. The versatile E3-E3 super-assembly may therefore underlie widespread ubiquitylation.
External links	Nature / PubMed:33536622 / PubMed Central
Methods	EM (single particle)
Resolution	3.6 - 9.7 Å
Structure data	EMDB-12004: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 ligase superassembly. NEDD8-CUL1-RBX1-SKP1-FBXW7-Cyclin E-ARIH1-UBE2L3~Ub. Pre-Transition State 1 Method: EM (single particle) / Resolution: 4.5 Å EMDB-12005: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-SKP1-FBXW7-Cyclin E-ARIH1~Ub. post-Transition State 1 Method: EM (single particle) / Resolution: 8.09 Å EMDB-12006: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-SKP1-FBXW7-Cyclin E~Ub~ARIH1. Transition State 2 Method: EM (single particle) / Resolution: 3.62 Å EMDB-12036: Ubiquitin ligation to F-box protein targets by SCF-RBR E3-E3 super-assembly Method: EM (single particle) / Resolution: 9.7 Å 12037 7b5l EMDB-12037, PDB-7b5l: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-SKP1-SKP2-CKSHS1-Cyclin A-CDK2-p27-UBE2L3~Ub~ARIH1. Transition State 1 Method: EM (single particle) / Resolution: 3.8 Å EMDB-12038: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-SKP1-SKP2-CKSHS1-Cyclin A-CDK2-p27-UBE2L3~Ub~ARIH1. Transition State 1 Method: EM (single particle) / Resolution: 3.83 Å EMDB-12039: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-SKP1-FBXW7-Cyclin E~Ub~ARIH1. Transition State 2 Method: EM (single particle) / Resolution: 4.48 Å 12040 7b5m EMDB-12040, PDB-7b5m: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-SKP1-SKP2-CKSHS1-p27~Ub~ARIH1. Transition State 2 Method: EM (single particle) / Resolution: 3.91 Å 12041 7b5n EMDB-12041: Focused map-catalytic side. Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-UBE2L3~Ub~ARIH1. PDB-7b5n: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: NEDD8-CUL1-RBX1-UBE2L3~Ub~ARIH1. Method: EM (single particle) / Resolution: 3.6 Å 12048 7b5r EMDB-12048: Focused map- CyclinA-CDK2-class. Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-SKP1-SKP2-CKSHS1-Cyclin A-CDK2-p27. Transition State 1 PDB-7b5r: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-SKP1-SKP2-CKSHS1-Cyclin A-CDK2-p27 Method: EM (single particle) / Resolution: 3.8 Å 12050 7b5s EMDB-12050: Focused map- Cullin scaffold. Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-ARIH1 Ariadne. Transition State 1 PDB-7b5s: Ubiquitin ligation to F-box protein substrates by SCF-RBR E3-E3 super-assembly: CUL1-RBX1-ARIH1 Ariadne. Transition State 1 Method: EM (single particle) / Resolution: 3.6 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-SY8: 5-azanylpentan-2-one
Source	homo sapiens (human)
Keywords	LIGASE / ubiquitin / ubiquitin ligase / E3 ligase / F-box protein / RBR ligase / Cullin-RING-Ligase / CRL / SCF / NEDD8 / Post-translational modification / ubiquitylation