2J0Q

The crystal structure of the Exon Junction Complex at 3.2 A resolution

Summary for 2J0Q

• Entry DOI: 10.2210/pdb2j0q/pdb
• Related: 1P27 2J0S 2J0U
• Descriptor: ATP-DEPENDENT RNA HELICASE DDX48, PROTEIN MAGO NASHI HOMOLOG, RNA-BINDING PROTEIN 8A, ... (8 entities in total)
• Functional Keywords: hydrolase, mrna processing, mrna splicing, mrna transport, nuclear protein, dead-box helicase, rna-binding
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: P38919 P61326 Q9Y5S9; Cytoplasm, perinuclear region: O15234
• Total number of polymer chains: 10
• Total formula weight: 198964.38

Authors

Bono, F.,Ebert, J.,Lorentzen, E.,Conti, E. (deposition date: 2006-08-04, release date: 2006-08-30, Last modification date: 2023-12-13)

Primary citation

Bono, F.,Ebert, J.,Lorentzen, E.,Conti, E.
The Crystal Structure of the Exon Junction Complex Reveals How It Maintains a Stable Grip on Mrna.
Cell(Cambridge,Mass.), 126:713-, 2006

PubMed Abstract: The exon junction complex (EJC) plays a major role in posttranscriptional regulation of mRNA in metazoa. The EJC is deposited onto mRNA during splicing and is transported to the cytoplasm where it influences translation, surveillance, and localization of the spliced mRNA. The complex is formed by the association of four proteins (eIF4AIII, Barentsz [Btz], Mago, and Y14), mRNA, and ATP. The 2.2 A resolution structure of the EJC reveals how it stably locks onto mRNA. The DEAD-box protein eIF4AIII encloses an ATP molecule and provides the binding sites for six ribonucleotides. Btz wraps around eIF4AIII and stacks against the 5' nucleotide. An intertwined network of interactions anchors Mago-Y14 and Btz at the interface between the two domains of eIF4AIII, effectively stabilizing the ATP bound state. Comparison with the structure of the eIF4AIII-Btz subcomplex that we have also determined reveals that large conformational changes are required upon EJC assembly and disassembly.

PubMed: 16923391
DOI: 10.1016/J.CELL.2006.08.006

Experimental method

X-RAY DIFFRACTION (3.2 Å)