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Wiley, FEBS Letters, 19(587), p. 3243-3248, 2013

DOI: 10.1016/j.febslet.2013.08.018

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Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function

Journal article published in 2013 by Jae-Hyeong Ko, Yane-Shih Wang ORCID, Akiyoshi Nakamura, Li-Tao Guo, Dieter Söll, Takuya Umehara
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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 PylRS amino acid complex show that the small pocket size and π-interaction play an important role in specific recognition of Phe and the engineered PylRS active site resembles that of E. coli PheRS.