7WRU

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

Summary for 7WRU

• Entry DOI: 10.2210/pdb7wru/pdb
• Descriptor: Glutamyl-tRNA synthetase, MERCURY (II) ION (3 entities in total)
• Functional Keywords: vertabrate, trna synthetase, translation
• Biological source: Gallus gallus (chicken)
• Total number of polymer chains: 1
• Total formula weight: 61561.16

Authors

Chung, S.,Cho, Y. (deposition date: 2022-01-27, release date: 2022-11-23, Last modification date: 2023-11-29)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)