Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Pro...
Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase
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United States: Public Library of Science
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English
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United States: Public Library of Science
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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 enantioselectivity. We now show, using nuclear magnetic re...
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Full title
Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase
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TN_cdi_plos_journals_1797504480
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_plos_journals_1797504480
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ISSN
1545-7885,1544-9173
E-ISSN
1545-7885
DOI
10.1371/journal.pbio.1002465
