7WRU
Crystal structure of the apo chicken glutamyl-tRNA synthetase 1 (EARS1)
7WRU の概要
エントリーDOI | 10.2210/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 | |
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: 36347866DOI: 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) |
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