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	Assembly status transition offers an avenue for activity modulation of a supramolecular enzyme.
ジャーナル・号・ページ	Elife, Vol. 10, Year 2021
掲載日	2021年12月13日
著者	Yao Chen / Weiya Xu / Shuwei Yu / Kang Ni / Guangbiao She / Xiaodong Ye / Qiong Xing / Jian Zhao / Chengdong Huang /
PubMed 要旨	Nature has evolved many supramolecular proteins assembled in certain, sometimes even seemingly oversophisticated, morphological manners. The rationale behind such evolutionary efforts is often poorly ...Nature has evolved many supramolecular proteins assembled in certain, sometimes even seemingly oversophisticated, morphological manners. The rationale behind such evolutionary efforts is often poorly understood. Here, we provide atomic-resolution insights into how the dynamic building of a structurally complex enzyme with higher order symmetry offers amenability to intricate regulation. We have established the functional coupling between enzymatic activity and protein morphological states of glutamine synthetase (GS), an old multi-subunit enzyme essential for cellular nitrogen metabolism. Cryo-EM structure determination of GS in both the catalytically active and inactive assembly states allows us to reveal an unanticipated self-assembly-induced disorder-order transition paradigm, in which the remote interactions between two subcomplex entities significantly rigidify the otherwise structurally fluctuating active sites, thereby regulating activity. We further show in vivo evidences that how the enzyme morphology transitions could be modulated by cellular factors on demand. Collectively, our data present an example of how assembly status transition offers an avenue for activity modulation, and sharpens our mechanistic understanding of the complex functional and regulatory properties of supramolecular enzymes.
リンク	Elife / PubMed:34898426 / PubMed Central
手法	EM (単粒子)
解像度	2.9 - 3.5 Å
構造データ	31711 7v4h EMDB-31711, PDB-7v4h: Cryo-EM Structure of Glycine max glutamine synthetase GmGS Beta2 手法: EM (単粒子) / 解像度: 2.9 Å 31712 7v4i EMDB-31712, PDB-7v4i: Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb decamer assembly 手法: EM (単粒子) / 解像度: 3.3 Å 31713 7v4j EMDB-31713, PDB-7v4j: Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State I 手法: EM (単粒子) / 解像度: 3.5 Å 31714 7v4k EMDB-31714, PDB-7v4k: Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State II 手法: EM (単粒子) 31715 7v4l EMDB-31715, PDB-7v4l: Cryo-EM Structure of Camellia sinensis glutamine synthetase CsGSIb inactive Pentamer State III 手法: EM (単粒子) / 解像度: 3.4 Å
由来	glycine max (ダイズ) camellia sinensis (チャ)
キーワード	LIGASE (リガーゼ) / supramolecular enzyme / glutamine synthetase (グルタミンシンテターゼ) / Glycine max / PLANT PROTEIN (植物) / IMMUNE SYSTEM (免疫系) / Camellia sinensis (チャノキ)