Literature DB >> 33069069

An orthogonal seryl-tRNA synthetase/tRNA pair for noncanonical amino acid mutagenesis in Escherichia coli.

Claudio Zambaldo1, Minseob Koh1, Fariborz Nasertorabi2, Gye Won Han2, Abhishek Chatterjee3, Raymond C Stevens4, Peter G Schultz5.   

Abstract

We report the development of the orthogonal amber-suppressor pair Archaeoglobus fulgidus seryl-tRNA (Af-tRNASer)/Methanosarcina mazei seryl-tRNA synthetase (MmSerRS) in Escherichia coli. Furthermore, the crystal structure of MmSerRS was solved at 1.45 Å resolution, which should enable structure-guided engineering of its active site to genetically encode small, polar noncanonical amino acids (ncAAs).
Copyright © 2020 Elsevier Ltd. All rights reserved.

Entities:  

Keywords:  E. coli orthogonality; Genetic code expansion; Non-canonical amino acids; Seryl-tRNA synthetase; X-ray crystallography

Mesh:

Substances:

Year:  2020        PMID: 33069069      PMCID: PMC9462667          DOI: 10.1016/j.bmc.2020.115662

Source DB:  PubMed          Journal:  Bioorg Med Chem        ISSN: 0968-0896            Impact factor:   3.461


  37 in total

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Authors:  Katherine T Grasso; Soumya Jyoti Singha Roy; Arianna O Osgood; Megan Jin Rae Yeo; Chintan Soni; Christen M Hillenbrand; Elise D Ficaretta; Abhishek Chatterjee
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3.  Rational Design of Aptamer-Tagged tRNAs.

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