PMID:12876372
| Citation |
Rupert, PB, Xiao, H and Ferré-D'Amaré, AR (2003) U1A RNA-binding domain at 1.8 A resolution. Acta Crystallogr. D Biol. Crystallogr. 59:1521-4 |
|---|---|
| Abstract |
The human U1A RNA-binding domain (RBD1) adopts one of the most common protein folds, the RNA-recognition motif, and is a paradigm for understanding RNA-protein interactions. A 2.8 A resolution structure of the unbound RBD1 has previously been determined [Nagai et al. (1990). Nature (London), 348, 515-520] and revealed a well defined alpha/beta core with disordered termini. Using a longer construct, a 1.8 A resolution structure of the unbound domain was determined that reveals an ordered C-terminal helix. The presence of this helix is consistent with a solution structure of the free domain [Avis et al. (1996). J. Mol. Biol. 257, 398-411]; however, in the solution structure the helix occludes the RNA-binding surface. In the present structure, the helix occupies a position similar to that seen in a 1.9 A resolution RNA-RBD1 complex structure [Oubridge et al. (1994). Nature (London), 372, 432-438]. The crystals in this study were grown from 2.2 M sodium malonate. It is possible that the high salt concentration helps to orient the C-terminal helix in the RNA-bound conformation by strengthening hydrophobic interactions between the buried face of the helix and the alpha/beta core of the protein. Alternatively, the malonate (several molecules of which are bound in the vicinity of the RNA-binding surface) may mimic RNA. |
| Links | |
| Keywords |
Amino Acid Motifs; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Humans; Models, Molecular; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; RNA/chemistry; RNA-Binding Proteins; Recombinant Proteins/chemistry; Ribonucleoprotein, U1 Small Nuclear/chemistry |
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