1EKZ

NMR STRUCTURE OF THE COMPLEX BETWEEN THE THIRD DSRBD FROM DROSOPHILA STAUFEN AND A RNA HAIRPIN

Summary for 1EKZ

• Entry DOI: 10.2210/pdb1ekz/pdb
• NMR Information: BMRB: 4894
• Descriptor: STAUFEN DOUBLE-STRANDED RNA BINDING DOMAIN, MATERNAL EFFECT PROTEIN (STAUFEN) (2 entities in total)
• Functional Keywords: protein/rna, protein dsrbd, drosophila, rna hairpin, cell cycle-rna complex, cell cycle/rna
• Biological source: Drosophila melanogaster (fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 18076.69

Authors

Ramos, A.,Grunert, S.,Bycroft, M.,St Johnston, D.,Varani, G. (deposition date: 2000-03-11, release date: 2000-08-21, Last modification date: 2024-05-22)

Primary citation

Ramos, A.,Grunert, S.,Adams, J.,Micklem, D.R.,Proctor, M.R.,Freund, S.,Bycroft, M.,St Johnston, D.,Varani, G.
RNA recognition by a Staufen double-stranded RNA-binding domain.
EMBO J., 19:997-1009, 2000

PubMed Abstract: The double-stranded RNA-binding domain (dsRBD) is a common RNA-binding motif found in many proteins involved in RNA maturation and localization. To determine how this domain recognizes RNA, we have studied the third dsRBD from Drosophila Staufen. The domain binds optimally to RNA stem-loops containing 12 uninterrupted base pairs, and we have identified the amino acids required for this interaction. By mutating these residues in a staufen transgene, we show that the RNA-binding activity of dsRBD3 is required in vivo for Staufen-dependent localization of bicoid and oskar mRNAs. Using high-resolution NMR, we have determined the structure of the complex between dsRBD3 and an RNA stem-loop. The dsRBD recognizes the shape of A-form dsRNA through interactions between conserved residues within loop 2 and the minor groove, and between loop 4 and the phosphodiester backbone across the adjacent major groove. In addition, helix alpha1 interacts with the single-stranded loop that caps the RNA helix. Interactions between helix alpha1 and single-stranded RNA may be important determinants of the specificity of dsRBD proteins.

PubMed: 10698941
DOI: 10.1093/emboj/19.5.997

Experimental method

SOLUTION NMR