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Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function.

ABSTRACT: Pyrrolysyl-tRNA synthetase (PylRS) is a class IIc aminoacyl-tRNA synthetase that is related to phenylalanyl-tRNA synthetase (PheRS). Genetic selection provided PylRS variants with a broad range of specificity for diverse non-canonical amino acids (ncAAs). One variant is a specific phenylalanine-incorporating enzyme. Structural models of the PylRSamino acid complex show that the small pocket size and ?-interaction play an important role in specific recognition of Phe and the engineered PylRS active site resembles that of Escherichia coli PheRS.

SUBMITTER: Ko JH

PROVIDER: S-EPMC3778162 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function.

Ko Jae-hyeong JH Wang Yane-Shih YS Nakamura Akiyoshi A Guo Li-Tao LT Söll Dieter D Umehara Takuya T

FEBS letters 20130828 19

Pyrrolysyl-tRNA synthetase (PylRS) is a class IIc aminoacyl-tRNA synthetase that is related to phenylalanyl-tRNA synthetase (PheRS). Genetic selection provided PylRS variants with a broad range of specificity for diverse non-canonical amino acids (ncAAs). One variant is a specific phenylalanine-incorporating enzyme. Structural models of the PylRSamino acid complex show that the small pocket size and π-interaction play an important role in specific recognition of Phe and the engineered PylRS acti ...[more]

PMID: 23994531

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