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J Mol Biol. 2016 Sep 11;428(18):3570-3576. doi: 10.1016/j.jmb.2016.05.011. Epub 2016 May 16.

Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome.

Author information

1
Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR7104, INSERM U964, 1 rue Laurent Fries, 67404 Illkirch-Graffenstaden, France.
2
Université de Strasbourg, 4 Rue Blaise Pascal, 67081 Strasbourg, France.
3
Laboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
4
Institute of Organic Chemistry, Leopold Franzens University, Innrain 80/82, A-6020, Innsbruck, Austria.
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Contributed equally

Abstract

Eukaryotic translation initiation factor eIF5A promotes protein synthesis by resolving polyproline-induced ribosomal stalling. Here, we report a 3.25-Å resolution crystal structure of eIF5A bound to the yeast 80S ribosome. The structure reveals a previously unseen conformation of an eIF5A-ribosome complex and highlights a possible functional link between conformational changes of the ribosome during protein synthesis and the eIF5A-ribosome association.

KEYWORDS:

crystallography; eIF5A; hypusine; ribosome; structure

PMID:
27196944
PMCID:
PMC5408928
DOI:
10.1016/j.jmb.2016.05.011
[Indexed for MEDLINE]
Free PMC Article

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