6KND

The C-terminal Domain of Translation Initiation Factor 5 at low pH

Summary for 6KND

• Entry DOI: 10.2210/pdb6knd/pdb
• Descriptor: Translation initiation factor eIF5 (2 entities in total)
• Functional Keywords: initiation factor, translation
• Biological source: Candida albicans
• Total number of polymer chains: 1
• Total formula weight: 18880.32

Authors

Jian, Y.,YuXin, Y.,Min, Y. (deposition date: 2019-08-05, release date: 2020-06-17, Last modification date: 2024-03-27)

Primary citation

Ye, Y.,Chen, M.,Kato, K.,Yao, M.
The pH-dependent conformational change of eukaryotic translation initiation factor 5: Insights into partner-binding manner.
Biochem.Biophys.Res.Commun., 519:186-191, 2019

PubMed Abstract: In the process of eukaryotic translation, the formation of preinitiation complex 43S, which consists of a 40S subunit, the eIF2-GTP-Met-tRNAi ternary complex, eIF3, eIF1, eIF1A, and eIF5, is essential for translational quality control. Of those factors, eIF5 promotes the hydrolysis of eIF2-bound GTP to release eIF2-GDP in the complex for the recycling of eIF2. eIF5 appears to bind to the β subunit of eIF2 (eIF2β) via an interaction between aromatic/acidic residue-rich regions (AA-boxes) in the C-terminal domain of eIF5 (eIF5CTD) and three lysine clusters (K-boxes) in the N-terminal domain of eIF2β (eIF2βNTD). However, the details of this interaction are unclear, due to the lack of a structure for the eIF5-eIF2β complex, and the unavailability of an intact structure of eIF5, in which the AA-boxes are always disordered, with high flexibility. In this study, we solved two crystal structures of eIF5CTD from Candida albicans, which for the first time showed the AA-box2 of eIF5 presenting as an ordered helical structure. The structures exhibited different arrangements of AA-box2 under different pH values, which may reflect the dynamic nature of the interactions of eIF5CTD, and eIF2βNTD in the preinitiation complex.

PubMed: 31492496
DOI: 10.1016/j.bbrc.2019.08.128

Experimental method

X-RAY DIFFRACTION (1.9 Å)