EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme.
ジャーナル・号・ページ	Mol Cell, Vol. 81, Issue 11, Page 2445-2459.e13, Year 2021
掲載日	2021年6月3日
著者	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 要旨	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.
リンク	Mol Cell / PubMed:33905682 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.95 - 19.2 Å
構造データ	EMDB-12537: Structure of human CTLH SR4 complex 手法: EM (単粒子) / 解像度: 6.6 Å EMDB-12538: Structure of endogenous yeast GID Ant complex 手法: EM (単粒子) / 解像度: 9.5 Å EMDB-12540: Structure of endogenous yeast Chelator-GID Ant complex 手法: EM (単粒子) / 解像度: 14.19 Å EMDB-12541: Structure of Apo Chelator-GID SR4 E3 ubiquitin ligase 手法: EM (単粒子) / 解像度: 13.5 Å EMDB-12542: Structure of human CTLH-WDR26 supramolecular assembly 手法: EM (単粒子) / 解像度: 19.2 Å EMDB-12545: Structure of supramolecular assembly and substrate receptor scaffolding modules of human CTLH-WDR26 complex 手法: EM (単粒子) / 解像度: 6.5 Å EMDB-12547: Structure of supramolecular assembly and substrate receptor scaffolding modules of human CTLH-MKLN1 complex 手法: EM (単粒子) / 解像度: 10.1 Å EMDB-12548: Structure of GID SR4 complex 手法: EM (単粒子) / 解像度: 7.96 Å EMDB-12557: Structure of yeast Chelator-GID SR4 E3 ubiquitin ligase bound to its tetrameric metabolic enzyme substrate Fbp1 手法: EM (単粒子) / 解像度: 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 手法: EM (単粒子) / 解像度: 3.5 Å 12560 7ns4 EMDB-12560, PDB-7ns4: Catalytic module of yeast Chelator-GID SR4 E3 ubiquitin ligase 手法: EM (単粒子) / 解像度: 3.9 Å 12563 7nsb EMDB-12563, PDB-7nsb: Supramolecular assembly module of yeast Chelator-GID SR4 E3 ubiquitin ligase 手法: EM (単粒子) / 解像度: 3.7 Å 12564 7nsc EMDB-12564, PDB-7nsc: Substrate receptor scaffolding module of human CTLH E3 ubiquitin ligase 手法: EM (単粒子) / 解像度: 3.3 Å PDB-7ns5: Structure of yeast Fbp1 (Fructose-1,6-bisphosphatase 1) 手法: X-RAY DIFFRACTION / 解像度: 1.95 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-PO4: PHOSPHATE ION / ホスファ-ト ChemComp-MG: Unknown entry / マグネシウムジカチオン ChemComp-HOH: WATER
由来	homo sapiens (ヒト) saccharomyces cerevisiae (パン酵母) saccharomyces cerevisiae (strain atcc 204508 / s288c) (パン酵母)
キーワード	LIGASE / GID / CTLH / ubiquitin / E3 ligase / supramolecular assembly / metabolism / gluconeogenesis / cryoEM / HYDROLASE