1EIF

EUKARYOTIC TRANSLATION INITIATION FACTOR 5A FROM METHANOCOCCUS JANNASCHII

1EIF の概要

• エントリーDOI: 10.2210/pdb1eif/pdb
• 分子名称: EUKARYOTIC TRANSLATION INITIATION FACTOR 5A (2 entities in total)
• 機能のキーワード: initiation factor, eif-5a, translation, ob-fold
• 由来する生物種: Methanocaldococcus jannaschii
• 細胞内の位置: Cytoplasm: Q58625
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14522.04

構造登録者

Kim, K.K.,Hung, L.W.,Yokota, H.,Kim, R.,Kim, S.H. (登録日: 1998-07-29, 公開日: 1998-10-14, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)