2iu1
From Proteopedia
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, resolution 1.80Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF EIF5 C-TERMINAL DOMAIN
Overview
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 pre-initiation complex assembly. The IF5-CTD interacts directly with the translation initiation factors eIF1, eIF2-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 eIF2B-epsilon (eIF2Bepsilon-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.
About this Structure
2IU1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5., Bieniossek C, Schutz P, Bumann M, Limacher A, Uson I, Baumann U, J Mol Biol. 2006 Jul 7;360(2):457-65. Epub 2006 May 24. PMID:16781736
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