1OO0

Crystal structure of the Drosophila Mago nashi-Y14 complex

Summary for 1OO0

• Entry DOI: 10.2210/pdb1oo0/pdb
• Descriptor: Mago nashi protein, CG8781-PA, STRONTIUM ION, ... (7 entities in total)
• Functional Keywords: rna recognition motif, splicing, protein complex, exon junction complex, signaling protein
• Biological source: Drosophila melanogaster (fruit fly); More
• Cellular location: Nucleus: P49028 Q9V535
• Total number of polymer chains: 2
• Total formula weight: 30698.30

Authors

Shi, H.,Xu, R.M. (deposition date: 2003-03-02, release date: 2003-05-27, Last modification date: 2024-02-14)

Primary citation

Shi, H.,Xu, R.M.
Crystal structure of the Drosophila Mago nashi-Y14 complex
Genes Dev., 17:971-976, 2003

PubMed Abstract: Pre-mRNA splicing is essential for generating mature mRNA and is also important for subsequent mRNA export and quality control. The splicing history is imprinted on spliced mRNA through the deposition of a splicing-dependent multiprotein complex, the exon junction complex (EJC), at approximately 20 nucleotides upstream of exon-exon junctions. The EJC is a dynamic structure containing proteins functioning in the nuclear export and nonsense-mediated decay of spliced mRNAs. Mago nashi (Mago) and Y14 are core components of the EJC, and they form a stable heterodimer that strongly associates with spliced mRNA. Here we report a 1.85 A-resolution structure of the Drosophila Mago-Y14 complex. Surprisingly, the structure shows that the canonical RNA-binding surface of the Y14 RNA recognition motif (RRM) is involved in extensive protein-protein interactions with Mago. This unexpected finding provides important insights for understanding the molecular mechanisms of EJC assembly and RRM-mediated protein-protein interactions.

PubMed: 12704080
DOI: 10.1101/gad.260403

Experimental method

X-RAY DIFFRACTION (1.85 Å)