Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase

D-aminoacyl-tRNA deacylase (DTD) removes D-amino acids mischarged on tRNAs and is thus implicated in enforcing homochirality in proteins. Previously, we proposed that selective capture of D-aminoacyl-tRNA by DTD’s invariant, cross-subunit Gly-cisPro motif forms the mechanistic basis for its enantios...

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Udgivet i:PLoS Biol
Main Authors: Routh, Satya Brata, Pawar, Komal Ishwar, Ahmad, Sadeem, Singh, Swati, Suma, Katta, Kumar, Mantu, Kuncha, Santosh Kumar, Yadav, Kranthikumar, Kruparani, Shobha P, Sankaranarayanan, Rajan
Format: Artigo
Sprog:Inglês
Udgivet: Public Library of Science 2016
Fag:
Research Article
Online adgang:https://ncbi.nlm.nih.gov/pmc/articles/PMC4880308/
https://ncbi.nlm.nih.gov/pubmed/27224426
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pbio.1002465
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