Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction
Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction
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DOI：
10.1073/pnas.0508728102
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发表时间：
2005-12-06
影响因子：
11.1
通讯作者：
Antson, AA
中科院分区：
文献类型：
--
作者：
Shevtsov, MB;Chen, YL;Antson, AA
在枯草芽孢杆菌中，抗TRAP蛋白（AT）响应于不带电荷的tRNA（Trp）的积累而产生。AT通过与色氨酸激活的trp RNA结合衰减蛋白（TRAP）结合并阻止其与几种mRNA的相互作用来调节参与色氨酸生物合成和转运的基因的表达。在这里，我们报告的X射线结构的AT在2.8埃分辨率，显示蛋白质亚基组装成紧密的三聚体。四个这样的三聚体进一步关联成一个12-亚基颗粒，其中单个三聚体通过双重和三重对称轴相关。十二个DnaJ样的富含半胱氨酸的锌结合结构域在十二聚体的表面上形成尖峰。现有的数据表明AT与11-亚基TRAP相互作用的几种可能的方式。AT锌结合结构域的灵活性可以帮助两个碱基错配分子之间的相互作用。
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA(Trp). AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 angstrom resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zinc-binding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains.