Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-10-06

AUTHORS

Malgorzata Dobosz-Bartoszek, Mark H Pinkerton, Zbyszek Otwinowski, Srinivas Chakravarthy, Dieter Söll, Paul R Copeland, Miljan Simonović

ABSTRACT

Selenocysteine is the only proteinogenic amino acid encoded by a recoded in-frame UGA codon that does not operate as the canonical opal stop codon. A specialized translation elongation factor, eEFSec in eukaryotes and SelB in prokaryotes, promotes selenocysteine incorporation into selenoproteins by a still poorly understood mechanism. Our structural and biochemical results reveal that four domains of human eEFSec fold into a chalice-like structure that has similar binding affinities for GDP, GTP and other guanine nucleotides. Surprisingly, unlike in eEF1A and EF-Tu, the guanine nucleotide exchange does not cause a major conformational change in domain 1 of eEFSec, but instead induces a swing of domain 4. We propose that eEFSec employs a non-canonical mechanism involving the distinct C-terminal domain 4 for the release of the selenocysteinyl-tRNA during decoding on the ribosome. More... »

PAGES

12941

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms12941

DOI

http://dx.doi.org/10.1038/ncomms12941

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1025781899

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/27708257


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