期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 360, 期 2, 页码 457-465出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2006.05.021
关键词
translation initiation; HEAT domain; eIF5; mulfi-factor complex
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 preinitiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-Met 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 weIF2B-epsilon (eIF2B epsilon-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. (c) 2006 Elsevier Ltd. All rights reserved.
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