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The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase

The crystal structure of an enzyme–substrate complex with histidyl-tRNA synthetase from Escherichia coli, ATP, and the amino acid analog histidinol is described and compared with the previously obtained enzyme–product complex with histidyl-adenylate. An active site arginine, Arg-259, unique to all h...

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Bibliographic Details
Published in:Proc Natl Acad Sci U S A
Main Authors: Arnez, John G., Augustine, John G., Moras, Dino, Francklyn, Christopher S.
Format: Artigo
Language:Inglês
Published: National Academy of Sciences 1997
Subjects:
Online Access:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC23771/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9207058/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.94.14.7144
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