Crystal structure of the C-terminal domain of S.cerevisiae eIF5

Journal of Molecular Biology
Zhiyi WeiWeimin Gong

Abstract

eIF5, a GTPase-activating protein (GAP) specific for eIF2, plays a critical role in pre-initiation complex assembly and correct AUG selection during eukaryotic translation initiation. eIF5 is involved in the formation of the multifactor complex (MFC), an important intermediate of the 43S pre-initiation complex. The C-terminal domain (CTD) of eIF5 functions as the structural core in the MFC assembly. Here we report the 1.5A crystal structure of eIF5-CTD, confirming that eIF5-CTD contains an atypical HEAT motif. In addition, analyzing the electrostatic potential and the distribution of conserved residues on the protein surface, we confirm and suggest some potential regions of interactions between eIF5-CTD and other eIFs. The structure of eIF5-CTD provides useful information in understanding the mechanism of the MFC assembly.

References

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Citations

May 21, 2010·Nature·Martin D Jennings, Graham D Pavitt
May 7, 2010·The Journal of Biological Chemistry·Jon R Lorsch, Thomas E Dever
May 15, 2010·Molecular & Cellular Proteomics : MCP·Friedrich FörsterWolfgang Baumeister
May 29, 2015·The Arabidopsis Book·Karen S Browning, Julia Bailey-Serres
Jul 28, 2016·Nucleic Acids Research·Martin D JenningsGraham D Pavitt
Jul 11, 2018·Wiley Interdisciplinary Reviews. RNA·Graham D Pavitt
Sep 23, 2006·The EMBO Journal·Chingakham Ranjit SinghKatsura Asano
May 18, 2016·Genetics·Thomas E DeverGraham D Pavitt
Jul 18, 2008·Biochemical Society Transactions·Sarah S Mohammad-QureshiGraham D Pavitt
Jun 12, 2012·Biochemical and Biophysical Research Communications·Zuoqi GaiMin Yao

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