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An evolved aminoacyl-tRNA synthetase with atypical polysubstrate specificity

Academic Article
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Overview

related to degree

  • Young, Travis Scott, Ph.D. in Chemical Biology, Scripps Research 2005 - 2010

authors

  • Young, D. D.
  • Young, Travis Scott
  • Jahnz, M.
  • Ahmad, Insha
  • Spraggon, G.
  • Schultz, Peter

publication date

  • March 2011

journal

  • Biochemistry  Journal

abstract

  • We have employed a rapid fluorescence-based screen to assess the polyspecificity of several aminoacyl-tRNA synthetases (aaRSs) against an array of unnatural amino acids. We discovered that a p-cyanophenylalanine specific aminoacyl-tRNA synthetase (pCNF-RS) has high substrate permissivity for unnatural amino acids, while maintaining its ability to discriminate against the 20 canonical amino acids. This orthogonal pCNF-RS, together with its cognate amber nonsense suppressor tRNA, is able to selectively incorporate 18 unnatural amino acids into proteins, including trifluoroketone-, alkynyl-, and halogen-substituted amino acids. In an attempt to improve our understanding of this polyspecificity, the X-ray crystal structure of the aaRS-p-cyanophenylalanine complex was determined. A comparison of this structure with those of other mutant aaRSs showed that both binding site size and other more subtle features control substrate polyspecificity.

subject areas

  • Alanine
  • Amino Acyl-tRNA Synthetases
  • Binding Sites
  • Crystallography, X-Ray
  • Escherichia coli
  • Models, Molecular
  • Nitriles
  • Protein Conformation
  • RNA, Transfer
  • Substrate Specificity
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Identity

PubMed Central ID

  • PMC3694404

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi101929e

PubMed ID

  • 21280675
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Additional Document Info

start page

  • 1894

end page

  • 1900

volume

  • 50

issue

  • 11

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