2IU1

Crystal structure of eIF5 C-terminal domain

2IU1 の概要

• エントリーDOI: 10.2210/pdb2iu1/pdb
• 分子名称: EUKARYOTIC TRANSLATION INITIATION FACTOR 5 (2 entities in total)
• 機能のキーワード: mfc, eif5, gtp-binding, phosphorylation, protein biosynthesis, translation inititation, initiation factor, nucleotide-binding, transcription
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24442.86

構造登録者

Bieniossek, C.,Schuetz, P.,Baumann, U. (登録日: 2006-05-26, 公開日: 2006-06-01, 最終更新日: 2024-05-08)

主引用文献

Bieniossek, C.,Schutz, P.,Bumann, M.,Limacher, A.,Uson, I.,Baumann, U.
The Crystal Structure of the Carboxy-Terminal Domain of Human Translation Initiation Factor Eif5.
J.Mol.Biol., 360:457-, 2006

PubMed Abstract: The carboxy-terminal domain (CTD) of eukaryotic initiation factor 5 (eIF5) plays a central role in the formation of the multifactor complex (MFC), an important intermediate for the 43 S pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-beta, and eIF3c, thus forming together with eIF2 bound Met-tRNA(i)(Met) the MFC. In this work we present the high resolution crystal structure of eIF5-CTD. This domain of the protein is exclusively composed out of alpha-helices and is homologous to the carboxy-terminal domain of eIF2B-epsilon (eIF2Bepsilon-CTD). The most striking difference in the two structures is an additional carboxy-terminal helix in eIF5. The binding sites of eIF2-beta, eIF3 and eIF1 were mapped onto the structure. eIF2-beta and eIF3 bind to non-overlapping patches of negative and positive electrostatic potential, respectively.

PubMed: 16781736
DOI: 10.1016/J.JMB.2006.05.021

実験手法

X-RAY DIFFRACTION (1.8 Å)