Ontology highlight
ABSTRACT:
SUBMITTER: Tian Q
PROVIDER: S-EPMC4357726 | biostudies-literature | 2015 Mar
REPOSITORIES: biostudies-literature
Tian Qingnan Q Wang Caiyan C Liu Yuhuan Y Xie Wei W
Nucleic acids research 20150226 5
Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in protein translation by linking tRNAs with cognate amino acids. Among all the tRNAs, only tRNA(His) bears a guanine base at position -1 (G-1), and it serves as a major recognition element for histidyl-tRNA synthetase (HisRS). Despite strong interests in the histidylation mechanism, the tRNA recognition and aminoacylation details are not fully understood. We herein present the 2.55 Å crystal structure of HisRS complexed with tRNA(His), whic ...[more]