Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
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DOI：
10.1038/45730
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发表时间：
1999-09-16
期刊：
影响因子：
64.8
通讯作者：
Gollnick, P
中科院分区：
文献类型：
--
作者：
Antson, AA;Dodson, EJ;Gollnick, P
FRP RNA结合衰减蛋白(TRAP)通过结合单链RNA来调节几种细菌色氨酸生物合成基因的表达。结合序列由11个三联体重复组成，主要是Gag，由两个或三个非保守核苷酸分隔，这里我们给出了TRAP和包含11个Gag三联体的53碱基单链RNA的复合体的晶体结构，揭示了每个三联体都容纳在由β链形成的结合口袋中。在复合体中，RNA具有扩展结构，没有任何碱基配对，并主要通过特定的蛋白质-碱基相互作用与蛋白质结合。圆形诱捕器上的11个捆绑口袋形成了一条直径约80埃的皮带。这种通过将RNA片段包围在蛋白质盘周围来阻止RNA片段的简单但优雅的机制既适用于TRAP与新生RNA结合时的转录，也适用于当TRAP与信使RNA的非编码前导区内的相同序列结合时的翻译。
The frp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes of several bacilli by binding single-stranded RNA. The binding sequence is composed of eleven triplet repeats, predominantly GAG, separated by two or three non-conserved nucleotides, Here we present the crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets, revealing that each triplet is accommodated in a binding pocket formed by beta-strands. In the complex, the RNA has an extended structure without any base-pairing and binds to the protein mostly by specific protein-base interactions. Eleven binding pockets on the circular TRAP Il-mer form a belt with a diameter of about 80 Angstrom. This simple but elegant mechanism of arresting the RNA segment by encircling it around a protein disk is applicable to both transcription, when TRAP binds the nascent RNA, and to translation, when TRAP binds the same sequence within a non-coding leader region of the messenger RNA.