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7WRU

Crystal structure of the apo chicken glutamyl-tRNA synthetase 1 (EARS1)

7WRU の概要
エントリーDOI10.2210/pdb7wru/pdb
分子名称Glutamyl-tRNA synthetase, MERCURY (II) ION (3 entities in total)
機能のキーワードvertabrate, trna synthetase, translation
由来する生物種Gallus gallus (chicken)
タンパク質・核酸の鎖数1
化学式量合計61561.16
構造登録者
Chung, S.,Cho, Y. (登録日: 2022-01-27, 公開日: 2022-11-23, 最終更新日: 2023-11-29)
主引用文献Chung, S.,Kang, M.S.,Alimbetov, D.S.,Mun, G.I.,Yunn, N.O.,Kim, Y.,Kim, B.G.,Wie, M.,Lee, E.A.,Ra, J.S.,Oh, J.M.,Lee, D.,Lee, K.,Kim, J.,Han, S.H.,Kim, K.T.,Chung, W.K.,Nam, K.H.,Park, J.,Lee, B.,Kim, S.,Zhao, W.,Ryu, S.H.,Lee, Y.S.,Myung, K.,Cho, Y.
Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1.
Nat Commun, 13:6732-6732, 2022
Cited by
PubMed Abstract: Aminoacyl-tRNA synthetases (ARSs) have evolved to acquire various additional domains. These domains allow ARSs to communicate with other cellular proteins in order to promote non-translational functions. Vertebrate cytoplasmic isoleucyl-tRNA synthetases (IARS1s) have an uncharacterized unique domain, UNE-I. Here, we present the crystal structure of the chicken IARS1 UNE-I complexed with glutamyl-tRNA synthetase 1 (EARS1). UNE-I consists of tandem ubiquitin regulatory X (UBX) domains that interact with a distinct hairpin loop on EARS1 and protect its neighboring proteins in the multi-synthetase complex from degradation. Phosphomimetic mutation of the two serine residues in the hairpin loop releases IARS1 from the complex. IARS1 interacts with BRCA1 in the nucleus, regulates its stability by inhibiting ubiquitylation via the UBX domains, and controls DNA repair function.
PubMed: 36347866
DOI: 10.1038/s41467-022-34612-y
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 7wru
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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