Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase

To achieve accurate aminoacylation of tRNAs with their cognate amino acids, errors in aminoacylation are corrected by the “editing” mechanism in several aminoacyl-tRNA synthetases. Phenylalanyl-tRNA synthetase (PheRS) hydrolyzes, or edits, misformed tyrosyl-tRNA with its editing domain in the β subu...

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Main Authors: Sasaki, Hiroshi M., Sekine, Shun-ichi, Sengoku, Toru, Fukunaga, Ryuya, Hattori, Motoyuki, Utsunomiya, Yukiko, Kuroishi, Chizu, Kuramitsu, Seiki, Shirouzu, Mikako, Yokoyama, Shigeyuki
Format: Artigo
Sprog:Inglês
Udgivet: National Academy of Sciences 2006
Fag:
Biological Sciences
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1595422/
https://ncbi.nlm.nih.gov/pubmed/17003130
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0603182103
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