NMR-based solution structure of the Caulobacter crescentus ProXp-ala trans-editing enzyme.

ABSTRACT: ProXp-ala is a key component of the translational machinery in all three Domains of life. This enzyme helps to maintain the fidelity of proline codon translation through aminoacyl-tRNA^Pro proofreading. In the first step of tRNA aminoacylation, the cognate aminoacyl-tRNA synthetase (aaRS) binds and activates an amino acid in the enzyme's synthetic active site. If a non-cognate amino acid passes this first selection step and is charged onto the tRNA, a distinct aaRS editing active site may recognize the mischarged tRNA and deacylate it. Alternatively, this editing reaction may be carried out by a separate enzyme that deacylates the mischarged tRNA in trans. ProXp-ala is responsible for editing Ala mischarged onto tRNA^Pro. Since trans-editing domains such as ProXp-ala bi

SUBMITTER: Duran AD 

PROVIDER: S-EPMC11511748 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature