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2HYI

Structure of the human exon junction complex with a trapped DEAD-box helicase bound to RNA

Summary for 2HYI
Entry DOI10.2210/pdb2hyi/pdb
Related1p27 2db3 2hxy
Descriptor5'-R(*UP*UP*UP*UP*UP*U)-3', Protein mago nashi homolog, RNA-binding protein 8A, ... (8 entities in total)
Functional Keywordsexon junction, splicing, mrna processing, translation, dead-box atpase, nonsense mediated decay, hydrolase-rna binding protein-rna complex, hydrolase/rna binding protein/rna
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus: P61326 Q9Y5S9 P38919
Cytoplasm, perinuclear region: O15234
Total number of polymer chains10
Total formula weight172982.64
Authors
Andersen, C.B.F.,Le Hir, H.,Andersen, G.R. (deposition date: 2006-08-06, release date: 2006-08-15, Last modification date: 2024-02-21)
Primary citationAndersen, C.B.F.,Ballut, L.,Johansen, J.S.,Chamieh, H.,Nielsen, K.H.,Oliveira, C.L.,Pedersen, J.S.,Seraphin, B.,Le Hir, H.,Andersen, G.R.
Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.
Science, 313:1968-1972, 2006
Cited by
PubMed Abstract: 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.
PubMed: 16931718
DOI: 10.1126/science.1131981
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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数据于2025-08-27公开中

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