Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-12

AUTHORS

Tateki Suzuki, Corwin Miller, Li-Tao Guo, Joanne M L Ho, David I Bryson, Yane-Shih Wang, David R Liu, Dieter Söll

ABSTRACT

Pyrrolysyl-tRNA synthetase (PylRS) is a major tool in genetic code expansion using noncanonical amino acids, yet its structure and function are not completely understood. Here we describe the crystal structure of the previously uncharacterized essential N-terminal domain of this unique enzyme in complex with tRNAPyl. This structure explains why PylRS remains orthogonal in a broad range of organisms, from bacteria to humans. The structure also illustrates why tRNAPyl recognition by PylRS is anticodon independent: the anticodon does not contact the enzyme. Then, using standard microbiological culture equipment, we established a new method for laboratory evolution-a noncontinuous counterpart of the previously developed phage-assisted continuous evolution. With this method, we evolved novel PylRS variants with enhanced activity and amino acid specificity. Finally, we employed an evolved PylRS variant to determine its N-terminal domain structure and show how its mutations improve PylRS activity in the genetic encoding of a noncanonical amino acid. More... »

PAGES

1261-1266

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nchembio.2497

DOI

http://dx.doi.org/10.1038/nchembio.2497

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1092236982

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/29035363


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