Ontology highlight
ABSTRACT:
SUBMITTER: Yu Z
PROVIDER: S-EPMC10164559 | biostudies-literature | 2023 May
REPOSITORIES: biostudies-literature
Yu Zhaoli Z Wu Zihan Z Li Ye Y Hao Qiang Q Cao Xiaofeng X Blaha Gregor M GM Lin Jinzhong J Lu Guoliang G
Nucleic acids research 20230501 8
Two types of glycyl-tRNA synthetase (GlyRS) are known, the α2 and the α2β2 GlyRSs. Both types of synthetase employ a class II catalytic domain to aminoacylate tRNAGly. In plastids and some bacteria, the α and β subunits are fused and are designated as (αβ)2 GlyRSs. While the tRNA recognition and aminoacylation mechanisms are well understood for α2 GlyRSs, little is known about the mechanisms for α2β2/(αβ)2 GlyRSs. Here we describe structures of the (αβ)2 GlyRS from Oryza sativa chloroplast by it ...[more]