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	GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
Journal, issue, pages	Mol Cell, Vol. 81, Issue 11, Page 2445-2459.e13, Year 2021
Publish date	Jun 3, 2021
Authors	Dawafuti Sherpa / Jakub Chrustowicz / Shuai Qiao / Christine R Langlois / Laura A Hehl / Karthik Varma Gottemukkala / Fynn M Hansen / Ozge Karayel / Susanne von Gronau / J Rajan Prabu / Matthias Mann / Arno F Alpi / Brenda A Schulman /
PubMed Abstract	How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of ...How are E3 ubiquitin ligases configured to match substrate quaternary structures? Here, by studying the yeast GID complex (mutation of which causes deficiency in glucose-induced degradation of gluconeogenic enzymes), we discover supramolecular chelate assembly as an E3 ligase strategy for targeting an oligomeric substrate. Cryoelectron microscopy (cryo-EM) structures show that, to bind the tetrameric substrate fructose-1,6-bisphosphatase (Fbp1), two minimally functional GID E3s assemble into the 20-protein Chelator-GID, which resembles an organometallic supramolecular chelate. The Chelator-GID assembly avidly binds multiple Fbp1 degrons so that multiple Fbp1 protomers are simultaneously ubiquitylated at lysines near the allosteric and substrate binding sites. Importantly, key structural and biochemical features, including capacity for supramolecular assembly, are preserved in the human ortholog, the CTLH E3. Based on our integrative structural, biochemical, and cell biological data, we propose that higher-order E3 ligase assembly generally enables multipronged targeting, capable of simultaneously incapacitating multiple protomers and functionalities of oligomeric substrates.
External links	Mol Cell / PubMed:33905682 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.95 - 19.2 Å
Structure data	EMDB-12537: Structure of human CTLH SR4 complex Method: EM (single particle) / Resolution: 6.6 Å EMDB-12538: Structure of endogenous yeast GID Ant complex Method: EM (single particle) / Resolution: 9.5 Å EMDB-12540: Structure of endogenous yeast Chelator-GID Ant complex Method: EM (single particle) / Resolution: 14.19 Å EMDB-12541: Structure of Apo Chelator-GID SR4 E3 ubiquitin ligase Method: EM (single particle) / Resolution: 13.5 Å EMDB-12542: Structure of human CTLH-WDR26 supramolecular assembly Method: EM (single particle) / Resolution: 19.2 Å EMDB-12545: Structure of supramolecular assembly and substrate receptor scaffolding modules of human CTLH-WDR26 complex Method: EM (single particle) / Resolution: 6.5 Å EMDB-12547: Structure of supramolecular assembly and substrate receptor scaffolding modules of human CTLH-MKLN1 complex Method: EM (single particle) / Resolution: 10.1 Å EMDB-12548: Structure of GID SR4 complex Method: EM (single particle) / Resolution: 7.96 Å EMDB-12557: Structure of yeast Chelator-GID SR4 E3 ubiquitin ligase bound to its tetrameric metabolic enzyme substrate Fbp1 Method: EM (single particle) / Resolution: 10.34 Å 12559 7ns3 EMDB-12559, PDB-7ns3: Substrate receptor scaffolding module of yeast Chelator-GID SR4 E3 ubiquitin ligase bound to Fbp1 substrate Method: EM (single particle) / Resolution: 3.5 Å 12560 7ns4 EMDB-12560, PDB-7ns4: Catalytic module of yeast Chelator-GID SR4 E3 ubiquitin ligase Method: EM (single particle) / Resolution: 3.9 Å 12563 7nsb EMDB-12563, PDB-7nsb: Supramolecular assembly module of yeast Chelator-GID SR4 E3 ubiquitin ligase Method: EM (single particle) / Resolution: 3.7 Å 12564 7nsc EMDB-12564, PDB-7nsc: Substrate receptor scaffolding module of human CTLH E3 ubiquitin ligase Method: EM (single particle) / Resolution: 3.3 Å PDB-7ns5: Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1) Method: X-RAY DIFFRACTION / Resolution: 1.95 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-PO4: PHOSPHATE ION ChemComp-MG: Unknown entry ChemComp-HOH: WATER
Source	homo sapiens (human) saccharomyces cerevisiae (brewer's yeast) saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
Keywords	LIGASE / GID / CTLH / ubiquitin / E3 ligase / supramolecular assembly / metabolism / gluconeogenesis / cryoEM / HYDROLASE