Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori.

ABSTRACT: The N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) plays a crucial role in the recognition of both tRNA^Asp and tRNA^Asn. Here, the first X-ray crystal structure of the N-terminal domain of this enzyme (ND-AspRS_1-104) from the human-pathogenic bacterium Helicobacter pylori is reported at 2.0 Å resolution. The apo form of H. pylori ND-AspRS_1-104 shares high structural similarity with the N-terminal anticodon-binding domains of the discriminating aspartyl-tRNA synthetase (D-AspRS) from Escherichia coli and ND-AspRS from Pseudomonas aeruginosa, allowing recognition elements to be proposed for tRNA^Asp and tRNA^Asn. It is proposed that a long loop (Arg77-Lys90) in this H. pylori doma

SUBMITTER: Songsiriritthigul C 

PROVIDER: S-EPMC5297925 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature