A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia
A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia
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Publisher
London: Nature Publishing Group UK
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Language
English
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Publisher
London: Nature Publishing Group UK
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Contents
D-aminoacyl-tRNA deacylase (DTD), a bacterial/eukaryotic
trans
-editing factor, removes
d
-amino acids mischarged on tRNAs and achiral glycine mischarged on tRNA
Ala
. An invariant cross-subunit Gly-
cis
Pro motif forms the mechanistic basis of
l
-amino acid rejection from the catalytic site. Here, we present the ident...
Alternative Titles
Full title
A chiral selectivity relaxed paralog of DTD for proofreading tRNA mischarging in Animalia
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TN_cdi_doaj_primary_oai_doaj_org_article_b9ffb78b9dda4f2c91cc1835bdec3b7f
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b9ffb78b9dda4f2c91cc1835bdec3b7f
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-017-02204-w
