Ontology highlight
ABSTRACT:
SUBMITTER: Songsiriritthigul C
PROVIDER: S-EPMC5297925 | biostudies-literature | 2017 Feb
REPOSITORIES: biostudies-literature
Songsiriritthigul Chomphunuch C Suebka Suwimon S Chen Chun Jung CJ Fuengfuloy Pitchayada P Chuawong Pitak P
Acta crystallographica. Section F, Structural biology communications 20170119 Pt 2
The N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) plays a crucial role in the recognition of both tRNA<sup>Asp</sup> and tRNA<sup>Asn</sup>. Here, the first X-ray crystal structure of the N-terminal domain of this enzyme (ND-AspRS<sub>1-104</sub>) from the human-pathogenic bacterium Helicobacter pylori is reported at 2.0 Å resolution. The apo form of H. pylori ND-AspRS<sub>1-104</sub> shares high structural similarity with the N-terminal anticod ...[more]