2EIF

Eukaryotic translation initiation factor 5A from Methanococcus jannaschii

Summary for 2EIF

• Entry DOI: 10.2210/pdb2eif/pdb
• Descriptor: PROTEIN (EUKARYOTIC TRANSLATION INITIATION FACTOR 5A) (2 entities in total)
• Functional Keywords: eif-5a, translation, ob-fold, structural genomics, bsgc structure funded by nih, protein structure initiative, psi, berkeley structural genomics center, gene regulation
• Biological source: Methanocaldococcus jannaschii
• Cellular location: Cytoplasm: Q58625
• Total number of polymer chains: 1
• Total formula weight: 14653.24

Authors

Kim, K.K.,Hung, L.W.,Kim, R.,Kim, S.H.,Berkeley Structural Genomics Center (BSGC) (deposition date: 1998-10-12, release date: 1999-10-12, Last modification date: 2023-08-23)

Primary citation

Kim, K.K.,Hung, L.W.,Yokota, H.,Kim, R.,Kim, S.H.
Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution.
Proc.Natl.Acad.Sci.USA, 95:10419-10424, 1998

PubMed 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.

PubMed: 9724718
DOI: 10.1073/pnas.95.18.10419

Experimental method

X-RAY DIFFRACTION (1.8 Å)