2J0U

The crystal structure of eIF4AIII-Barentsz complex at 3.0 A resolution

Summary for 2J0U

• Entry DOI: 10.2210/pdb2j0u/pdb
• Descriptor: ATP-DEPENDENT RNA HELICASE DDX48, PROTEIN CASC3 (3 entities in total)
• Functional Keywords: hydrolase, atp-binding, dna-binding, nuclear protein, rrna processing, dead-box helicase, nucleotide-binding, ejc, helicase, rna-binding, acetylation
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Nucleus: P38919 O15234; Cytoplasm, perinuclear region: P38919
• Total number of polymer chains: 3
• Total formula weight: 98913.14

Authors

Bono, F.,Ebert, J.,Lorentzen, E.,Conti, E. (deposition date: 2006-08-04, release date: 2006-09-06, 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 Mantains 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 Å)