4JHJ

Crystal structure of Danio rerio Slip1 in complex with Dbp5

Summary for 4JHJ

• Entry DOI: 10.2210/pdb4jhj/pdb
• Related: 2I2O 3FHC 3FHT 4JHK
• Descriptor: MIF4G domain-containing protein B, DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 19 (DBP5 homolog, yeast) (3 entities in total)
• Functional Keywords: dead-box helicase, mrna export, reca-like, rna-dependent atpase, ddx19, dead-box protein 19b, mrna transport, atp binding, helicase, hydrolase, nucleotide binding, rna binding, transport histone mrna processing, translation, 3'-utr, 3'-processing, nup214
• Biological source: Danio rerio (leopard danio,zebra danio,zebra fish); More
• Cellular location: Cytoplasm (By similarity): Q5EAQ1
• Total number of polymer chains: 4
• Total formula weight: 58580.46

Authors

Von Moeller, H.,Conti, E. (deposition date: 2013-03-05, release date: 2013-07-10, Last modification date: 2023-09-20)

Primary citation

von Moeller, H.,Lerner, R.,Ricciardi, A.,Basquin, C.,Marzluff, W.F.,Conti, E.
Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins.
Nucleic Acids Res., 41:7960-7971, 2013

PubMed Abstract: In metazoans, replication-dependent histone mRNAs end in a stem-loop structure instead of the poly(A) tail characteristic of all other mature mRNAs. This specialized 3' end is bound by stem-loop binding protein (SLBP), a protein that participates in the nuclear export and translation of histone mRNAs. The translational activity of SLBP is mediated by interaction with SLIP1, a middle domain of initiation factor 4G (MIF4G)-like protein that connects to translation initiation. We determined the 2.5 Å resolution crystal structure of zebrafish SLIP1 bound to the translation-activation domain of SLBP and identified the determinants of the recognition. We discovered a SLIP1-binding motif (SBM) in two additional proteins: the translation initiation factor eIF3g and the mRNA-export factor DBP5. We confirmed the binding of SLIP1 to DBP5 and eIF3g by pull-down assays and determined the 3.25 Å resolution structure of SLIP1 bound to the DBP5 SBM. The SBM-binding and homodimerization residues of SLIP1 are conserved in the MIF4G domain of CBP80/20-dependent translation initiation factor (CTIF). The results suggest how the SLIP1 homodimer or a SLIP1-CTIF heterodimer can function as platforms to bridge SLBP with SBM-containing proteins involved in different steps of mRNA metabolism.

PubMed: 23804756
DOI: 10.1093/nar/gkt558

Experimental method

X-RAY DIFFRACTION (3.25 Å)