4.5 Article

Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function

Journal

FEBS LETTERS
Volume 587, Issue 19, Pages 3243-3248

Publisher

WILEY
DOI: 10.1016/j.febslet.2013.08.018

Keywords

Pyrrolysyl-tRNA synthetase; Non-canonical amino acid; Phenylalanyl-tRNA synthetase; Superfolder green fluorescent protein

Funding

  1. National Institute for General Medical Sciences [GM22854]
  2. Defense Advanced Research Projects Agency [N66001-12-C-4020, N66001-12-C-4211]
  3. Grants-in-Aid for Scientific Research [24710231] Funding Source: KAKEN

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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 pi-interaction play an important role in specific recognition of Phe and the engineered PylRS active site resembles that of Escherichia coli PheRS. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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