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Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution.

Kim KK, Hung LW, Yokota H, Kim R, Kim SH
Proc Natl Acad Sci U S A 95 10419-24 (1998)
Cited: 79 times
EuropePMC logo PMID: 9724718

Abstract

Eukaryotic translation initiation factor 5A (eIF-5A) is a ubiquitous protein found in all eukaryotic cells. The protein is closely associated with cell proliferation in the G1-S stage of the cell cycle. Recent findings show that the eIF-5A proteins are highly expressed in tumor cells and act as a cofactor of the Rev protein in HIV-1-infected cells. The mature eIF is the only protein known to have the unusual amino acid hypusine, a post-translationally modified lysine. The crystal structure of eIF-5A from Methanococcus jannaschii (MJ eIF-5A) has been determined at 1.9 A and 1.8 A resolution in two crystal forms by using the multiple isomorphous replacement method and the multiwavelength anomalous diffraction method for the first crystal form and the molecular replacement method for the second crystal form. The structure consists of two folding domains, one of which is similar to the oligonucleotide-binding domain found in the prokaryotic cold shock protein and the translation initiation factor IF1 despite the absence of any significant sequence similarities. The 12 highly conserved amino acid residues found among eIF-5As include the hypusine site and form a long protruding loop at one end of the elongated molecule.

Reviews - 2eif mentioned but not cited (1)

  1. Functional significance of eIF5A and its hypusine modification in eukaryotes. Park MH, Nishimura K, Zanelli CF, Valentini SR. Amino Acids 38 491-500 (2010)

Articles - 2eif mentioned but not cited (5)



Reviews citing this publication (24)

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  12. Hypusine, a polyamine-derived amino acid critical for eukaryotic translation. Park MH, Wolff EC. J Biol Chem 293 18710-18718 (2018)
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  15. Is there a role for eIF5A in translation? Zanelli CF, Valentini SR. Amino Acids 33 351-358 (2007)
  16. Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A. Lassak J, Wilson DN, Jung K. Mol Microbiol 99 219-235 (2016)
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  23. Functions and Regulation of Translation Elongation Factors. Xu B, Liu L, Song G. Front Mol Biosci 8 816398 (2021)
  24. Hypusination, a Metabolic Posttranslational Modification of eIF5A in Plants during Development and Environmental Stress Responses. Pálfi P, Bakacsy L, Kovács H, Szepesi Á. Plants (Basel) 10 1261 (2021)

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