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4QEI

Two distinct conformational states of GlyRS captured in crystal lattice

4QEI の概要
エントリーDOI10.2210/pdb4qei/pdb
分子名称Glycine--tRNA ligase, tRNA-Gly-CCC-2-2, ADENOSINE MONOPHOSPHATE, ... (4 entities in total)
機能のキーワードaminoacyl-trna synthetase, glycylation, glycyl-trna synthetase, trna ligase, ligase-rna complex, ligase/rna
由来する生物種Homo sapiens (human)
詳細
細胞内の位置Cytoplasm : P41250
タンパク質・核酸の鎖数2
化学式量合計94430.99
構造登録者
Xie, W.,Qin, X.,Deng, X.,Zhang, Q.,Li, Q. (登録日: 2014-05-16, 公開日: 2015-05-20, 最終更新日: 2023-11-08)
主引用文献Deng, X.,Qin, X.,Chen, L.,Jia, Q.,Zhang, Y.,Zhang, Z.,Lei, D.,Ren, G.,Zhou, Z.,Wang, Z.,Li, Q.,Xie, W.
Large Conformational Changes of Insertion 3 in Human Glycyl-tRNA Synthetase (hGlyRS) during Catalysis
J.Biol.Chem., 291:5740-5752, 2016
Cited by
PubMed Abstract: Glycyl-tRNA synthetase (GlyRS) is the enzyme that covalently links glycine to cognate tRNA for translation. It is of great research interest because of its nonconserved quaternary structures, unique species-specific aminoacylation properties, and noncanonical functions in neurological diseases, but none of these is fully understood. We report two crystal structures of human GlyRS variants, in the free form and in complex with tRNA(Gly) respectively, and reveal new aspects of the glycylation mechanism. We discover that insertion 3 differs considerably in conformation in catalysis and that it acts like a "switch" and fully opens to allow tRNA to bind in a cross-subunit fashion. The flexibility of the protein is supported by molecular dynamics simulation, as well as enzymatic activity assays. The biophysical and biochemical studies suggest that human GlyRS may utilize its flexibility for both the traditional function (regulate tRNA binding) and alternative functions (roles in diseases).
PubMed: 26797133
DOI: 10.1074/jbc.M115.679126
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.875 Å)
構造検証レポート
Validation report summary of 4qei
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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