1DI2

CRYSTAL STRUCTURE OF A DSRNA-BINDING DOMAIN COMPLEXED WITH DSRNA: MOLECULAR BASIS OF DOUBLE-STRANDED RNA-PROTEIN INTERACTIONS

Summary for 1DI2

• Entry DOI: 10.2210/pdb1di2/pdb
• Descriptor: RNA (5'-R(*GP*GP*CP*GP*CP*GP*CP*GP*CP*C)-3'), DOUBLE STRANDED RNA BINDING PROTEIN A (3 entities in total)
• Functional Keywords: protein-rna complex, double stranded rna, protein-rna interactions, rna-bining protein, rna binding protein-rna complex, rna binding protein/rna
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 6
• Total formula weight: 28207.65

Authors

Ryter, J.M.,Schultz, S.C. (deposition date: 1999-11-28, release date: 1999-12-02, Last modification date: 2024-02-07)

Primary citation

Ryter, J.M.,Schultz, S.C.
Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA.
EMBO J., 17:7505-7513, 1998

PubMed Abstract: Protein interactions with double-stranded RNA (dsRNA) are critical for many cell processes; however, in contrast to protein-dsDNA interactions, surprisingly little is known about the molecular basis of protein-dsRNA interactions. A large and diverse class of proteins that bind dsRNA do so by utilizing an approximately 70 amino acid motif referred to as the dsRNA-binding domain (dsRBD). We have determined a 1.9 A resolution crystal structure of the second dsRBD of Xenopus laevis RNA-binding protein A complexed with dsRNA. The structure shows that the protein spans 16 bp of dsRNA, interacting with two successive minor grooves and across the intervening major groove on one face of a primarily A-form RNA helix. The nature of these interactions explains dsRBD specificity for dsRNA (over ssRNA or dsDNA) and the apparent lack of sequence specificity. Interestingly, the dsRBD fold resembles a portion of the conserved core structure of a family of polynucleotidyl transferases that includes RuvC, MuA transposase, retroviral integrase and RNase H. Structural comparisons of the dsRBD-dsRNA complex and models proposed for polynucleotidyl transferase-nucleic acid complexes suggest that similarities in nucleic acid binding also exist between these families of proteins.

PubMed: 9857205
DOI: 10.1093/emboj/17.24.7505

Experimental method

X-RAY DIFFRACTION (1.9 Å)