2EIF: Eukaryotic Translation Initiation Factor 5a From Methanococcus Jannaschii

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.
PDB ID: 2EIFDownload
MMDB ID: 12086
PDB Deposition Date: 1998/10/12
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 2EIF: monomeric; determined by author
Molecular Components in 2EIF
Label Count Molecule
Protein (1 molecule)
Protein (Eukaryotic Translation Initiation Factor 5A)(Gene symbol: MJ_RS06570)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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