Structure of the Exon Junction Core Complex with a Trapped DEAD-Box ATPase Bound to RNA
2006
Andersen, Christian B.F. | Ballut, Lionel | Johansen, Jesper S. | Chamieh, Hala | Nielsen, Klaus H. | Oliveira, Cristiano L.P. | Pedersen, Jan Skov | Séraphin, Bertrand | Le Hir, Hervé | Andersen, Gregers Rom
In higher eukaryotes, a multiprotein exon junction complex is deposited on spliced messenger RNAs. The complex is organized around a stable core, which serves as a binding platform for numerous factors that influence messenger RNA function. Here, we present the crystal structure of a tetrameric exon junction core complex containing the DEAD-box adenosine triphosphatase (ATPase) eukaryotic initiation factor 4AIII (eIF4AIII) bound to an ATP analog, MAGOH, Y14, a fragment of MLN51, and a polyuracil mRNA mimic. eIF4AIII interacts with the phosphate-ribose backbone of six consecutive nucleotides and prevents part of the bound RNA from being double stranded. The MAGOH and Y14 subunits lock eIF4AIII in a prehydrolysis state, and activation of the ATPase probably requires only modest conformational changes in eIF4AIII motif I.
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