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

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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Bibliographic Details
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: Online
Language:English
Published: Public Library of Science 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4880308/

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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4880308/

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