S16 throws a conformational switch during assembly of 30S 5′ domain

被引：0
作者：
Priya Ramaswamy
Sarah A Woodson
机构：
[1] Program in Cell,T. C. Jenkins Department of Biophysics
[2] Molecular and Developmental Biology and Biophysics,undefined
[3] Johns Hopkins University,undefined
[4] Johns Hopkins University,undefined
[5] Present address: Department of Biochemistry and Biophysics,undefined
[6] University of California San Francisco,undefined
[7] San Francisco,undefined
[8] California,undefined
[9] USA.,undefined
来源：
Nature Structural & Molecular Biology | 2009年 / 16卷
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摘要：
Ribosomal proteins are known to play an important role in determining rRNA structure. The body of the 30S ribosomal subunit is formed by the 16S rRNA 5′ domain. New data indicate that the assembly protein S16 discriminates between folding intermediates of the 5′ domain, increasing cooperative 30S assembly and stabilizing interactions at its decoding site.
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页码：438 / 445
页数：7
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