1eif
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(New page: 200px<br /><applet load="1eif" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eif, resolution 1.9Å" /> '''EUKARYOTIC TRANSLATIO...)
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Revision as of 11:54, 20 November 2007
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EUKARYOTIC TRANSLATION INITIATION FACTOR 5A FROM METHANOCOCCUS JANNASCHII
Overview
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.
About this Structure
1EIF is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
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. 1998 Sep 1;95(18):10419-24. PMID:9724718
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