5W2F

Crystal Structure of the C-terminal Domain of Human eIF2D at 1.4 A resolution

5W2F の概要

• エントリーDOI: 10.2210/pdb5w2f/pdb
• 分子名称: Eukaryotic translation initiation factor 2D, FORMIC ACID (3 entities in total)
• 機能のキーワード: re-initiation, ribosome, eif2, translation
• 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: 23199.92

構造登録者

Vaidya, A.T.,Lomakin, I.B.,Joseph, N.N.,Dmitriev, S.E.,Steitz, T.A. (登録日: 2017-06-06, 公開日: 2017-08-02, 最終更新日: 2024-03-13)

主引用文献

Vaidya, A.T.,Lomakin, I.B.,Joseph, N.N.,Dmitriev, S.E.,Steitz, T.A.
Crystal Structure of the C-terminal Domain of Human eIF2D and Its Implications on Eukaryotic Translation Initiation.
J. Mol. Biol., 429:2765-2771, 2017

PubMed Abstract: Protein synthesis is a key process in all living organisms. In eukaryotes, initiation factor 2 (eIF2) plays an important role in translation initiation as it selects and delivers the initiator tRNA to the small ribosomal subunit. Under stress conditions, phosphorylation of the α-subunit of eIF2 downregulates cellular protein synthesis. However, translation of certain mRNAs continues via the eIF2D-dependent non-canonical initiation pathway. The molecular mechanism of this process remains elusive. In addition, eIF2D plays a role in translation re-initiation and ribosome recycling. Currently, there has been no structural information of eIF2D. We have now determined the crystal structure of the C-terminal domains of eIF2D at 1.4-Å resolution. One domain has the fold similar to that of eIF1, which is crucial for the scanning and initiation codon selection. The second domain has a known SWIB/MDM2 fold, which was not observed before in other translation initiation factors. Our structure reveals atomic details of inter-domain interactions in the C-terminal part of eIF2D and sheds light on the possible role of these domains in eIF2D during translation.

PubMed: 28736176
DOI: 10.1016/j.jmb.2017.07.015

実験手法

X-RAY DIFFRACTION (1.4 Å)