Ontology highlight
ABSTRACT:
SUBMITTER: Moulinier L
PROVIDER: S-EPMC125622 | biostudies-literature | 2001 Sep
REPOSITORIES: biostudies-literature
Moulinier L L Eiler S S Eriani G G Gangloff J J Thierry J C JC Gabriel K K McClain W H WH Moras D D
The EMBO journal 20010901 18
The 2.6 A resolution crystal structure of an inactive complex between yeast tRNA(Asp) and Escherichia coli aspartyl-tRNA synthetase reveals the molecular details of a tRNA-induced mechanism that controls the specificity of the reaction. The dimer is asymmetric, with only one of the two bound tRNAs entering the active site cleft of its subunit. However, the flipping loop, which controls the proper positioning of the amino acid substrate, acts as a lid and prevents the correct positioning of the t ...[more]