一个细节的视图的核糖体活性部位:L11-RNA复合体的结构

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Updated: Jul 5, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses

Published on: February 25, 2011

B T Wimberly¹, R Guymon, J P McCutcheon

¹Department of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132, USA.

|May 25, 1999

概括

我们确定了一个关键的核糖体RNA-蛋白质复合物的晶体结构. 这揭示了像 thiostrepton 这样的抗生素是如何通过向核糖体蛋白质 L11.11 结合来抑制细菌蛋白质合成的.

科学领域:

结构生物学结构生物学
分子生物学分子生物学
微生物学微生物学

背景情况:

23S核糖体RNA (rRNA) 和核糖体蛋白L11形成了一个关键的核糖蛋白域.
这一域对于细菌蛋白质合成至关重要,并且是列抗生素的标.
抗生素耐药性机制往往涉及到这个领域的改变,影响延长因子的功能.

研究的目的:

为了阐明23S rRNA与核糖体蛋白L11结合的58核酸片段的高分辨率晶体结构.
了解rRNA与蛋白质L11之间的相互作用的结构基础.
调查斯特和相关抗生素的结合部位及其作用机制.

主要方法:

用X射线晶体学来确定核蛋白复合体的原子结构.
生物化学试验分析蛋白质-RNA相互作用.
突变分析以确定抗性部位.

主要成果:

晶体结构揭示了一个紧的RNA域,具有新的和熟悉的图案.
核糖体蛋白L11的C端域与RNA紧密结合,而N端域则充当开关.
在RNA和N端域之间有一个狭窄的裂被确定为thiostrepton和micrococcin的结合部位.

结论:

这种结构为蒂奥斯特普顿抗生素如何抑制细菌转化提供了分子基础.
L11的N端域作为一个开关,通过抗生素结合来调节.
了解这种相互作用是开发针对细菌核糖体的新抗生素的关键.

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