Crystal structure of the C-terminal domain of the ϵ subunit of human translation initiation factor eIF2B

Jia Wei1,Minze Jia2,Cheng Zhang2,Mingzhu Wang2,Feng Gao2,Hang Xu2,Weimin Gong2,

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Protein Cell ›› 2010, Vol. 1 ›› Issue (6) : 595-603. DOI: 10.1007/s13238-010-0070-6
Research articles

Crystal structure of the C-terminal domain of the ϵ subunit of human translation initiation factor eIF2B

  • Jia Wei1,Minze Jia2,Cheng Zhang2,Mingzhu Wang2,Feng Gao2,Hang Xu2,Weimin Gong2,
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Abstract

Eukaryotic translation initiation factor eIF2B, the guanine nucleotide exchange factor (GEF) for eIF2, catalyzes conversion of eIF2·GDP to eIF2·GTP. The eIF2B is composed of five subunits, α, β, γ, δ and ε, within which the ε subunit is responsible for catalyzing the guanine exchange reaction. Here we present the crystal structure of the C-terminal domain of human eIF2Bε (eIF2Bε-CTD) at 2.0-Å resolution. The structure resembles a HEAT motif and three charge-rich areas on its surface can be identified. When compared to yeast eIF2Bε-CTD, one area involves highly conserved AA boxes while the other two are only partially conserved. In addition, the previously reported mutations in human eIF2Bε-CTD, which are related to the loss of the GEF activity and human VWM disease, have been discussed. Based on the structure, most of such mutations tend to destabilize the HEAT motif.

Keywords

eukaryotic translation initiation factor 2B (eIF2B) / guanine nucleotide exchange factor (GEF) / crystal structure / HEAT motif / vanishing white matter (VWM)

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Jia Wei, Minze Jia, Cheng Zhang, Mingzhu Wang, Feng Gao, Hang Xu, Weimin Gong,. Crystal structure of the C-terminal domain of the ϵ subunit of human translation initiation factor eIF2B. Protein Cell, 2010, 1(6): 595‒603 https://doi.org/10.1007/s13238-010-0070-6
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