U1A RNA-binding domain at 1.8 Å resolution

被引:15
|
作者
Rupert, PB [1 ]
Xiao, H [1 ]
Ferré-D'Amaré, AR [1 ]
机构
[1] Fred Hutchinson Canc Res Ctr, Seattle, WA 98104 USA
关键词
D O I
10.1107/S0907444903011338
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom 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 Angstrom 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 Angstrom 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.
引用
收藏
页码:1521 / 1524
页数:4
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