The solution structure of ribosomal protein S4 Δ41 reveals two subdomains and a positively charged surface that may interact with RNA
The solution structure of ribosomal protein S4 Δ41 reveals two subdomains and a positively charged surface that may interact with RNA
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DOI：
10.1093/emboj/17.16.4559
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发表时间：
1998-08
期刊：
影响因子：
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通讯作者：
M. Markus;R. Gerstner;D. Draper;D. Torchia
中科院分区：
文献类型：
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作者：
M. Markus;R. Gerstner;D. Draper;D. Torchia
S4是在原核生物核糖体组装过程中最早与16 S RNA结合的蛋白质之一。嗜热脂肪芽孢杆菌S4的残基43-200（S4 Δ41）特异性结合16 S rRNA和α操纵子mRNA内的假结。作为理解S4如何识别和组织RNA的第一步，我们已经通过多维异谱核磁共振光谱解决了S4 Δ41在溶液中的结构。折叠由两个球状亚结构域组成，一个由四个螺旋组成，另一个由五链反平行β折叠和三个螺旋组成。尽管交联研究表明α2和α3螺旋之间的残基靠近RNA，但正电荷沿着两个亚结构域之间的缝隙的浓度表明这可能是RNA结合位点。与先前研究的L11 RNA结合结构域相反，S4 Δ41没有显示出快速的局部运动，这表明它具有较低的重折叠能力以适应RNA。独立测定的S4 Δ41的晶体结构显示出类似的特征，尽管与溶液结构相比，子域有小的旋转。溶液中各亚畴的相对取向有待于进一步的研究来验证。
S4 is one of the first proteins to bind to 16S RNA during assembly of the prokaryotic ribosome. Residues 43–200 of S4 from Bacillus stearothermophilus (S4 Δ41) bind specifically to both 16S rRNA and to a pseudoknot within the α operon mRNA. As a first step toward understanding how S4 recognizes and organizes RNA, we have solved the structure of S4 Δ41 in solution by multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The fold consists of two globular subdomains, one comprised of four helices and the other comprised of a five‐stranded antiparallel β‐sheet and three helices. Although cross‐linking studies suggest that residues between helices α2 and α3 are close to RNA, the concentration of positive charge along the crevice between the two subdomains suggests that this could be an RNA‐binding site. In contrast to the L11 RNA‐binding domain studied previously, S4 Δ41 shows no fast local motions, suggesting that it has less capacity for refolding to fit RNA. The independently determined crystal structure of S4 Δ41 shows similar features, although there is small rotation of the subdomains compared with the solution structure. The relative orientation of the subdomains in solution will be verified with further study.