Rak Alexey, Kalinin Alexander, Shcherbakov Dmitry, Bayer Peter
Department of Physical Biochemistry, Max-Planck-Institute for Molecular Physiology, Otto-Hahn-Str.11, 44227 Dortmund, Germany.
Biochem Biophys Res Commun. 2002 Dec 20;299(5):710-4. doi: 10.1016/s0006-291x(02)02721-3.
The solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli was determined by nuclear magnetic resonance with a RMSD of 0.6A. Yfia shows a global beta-alpha-beta-beta-beta-alpha folding topology similar to its homologue HI0257 of Haemophilus influenzae and the double-strand-binding domain of Drosophila Staufen protein. Yfia and HI0257 differ in their surface charges and in the composition of their flexible C-termini, indicating their specificity to different target molecules. Both proteins exhibit a hydrophobic and polar region, which probably functions as interaction site for protein complex formation. Despite their similarity to the dsRBD fold, Yfia does not bind to model fragments of 16S ribosomal RNA as determined by NMR titration and gel shift experiments.
通过核磁共振确定了大肠杆菌核糖体相关冷休克反应蛋白Yfia的溶液结构，其均方根偏差为0.6埃。Yfia呈现出一种整体的β-α-β-β-β-α折叠拓扑结构，类似于其同源物流感嗜血杆菌的HI0257以及果蝇Staufen蛋白的双链结合结构域。Yfia和HI0257在表面电荷和柔性C末端的组成上有所不同，这表明它们对不同靶分子具有特异性。两种蛋白质都有一个疏水和极性区域，这可能作为蛋白质复合物形成的相互作用位点。尽管Yfia与双链RNA结合结构域（dsRBD）折叠相似，但通过核磁共振滴定和凝胶迁移实验确定，Yfia不与16S核糖体RNA的模型片段结合。
