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分辨率为1.9埃的T4 regA翻译调节蛋白的晶体结构。

Crystal structure of the T4 regA translational regulator protein at 1.9 A resolution.

作者信息

Kang C, Chan R, Berger I, Lockshin C, Green L, Gold L, Rich A

机构信息

Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.

出版信息

Science. 1995 May 26;268(5214):1170-3. doi: 10.1126/science.7761833.

Abstract

The translational regulator protein regA is encoded by the T4 bacteriophage and binds to a region of messenger RNA (mRNA) that includes the initiator codon. RegA is unusual in that it represses the translation of about 35 early T4 mRNAs but does not affect nearly 200 other mRNAs. The crystal structure of regA was determined at 1.9 A resolution; the protein was shown to have an alpha-helical core and two regions with antiparallel beta sheets. One of these beta sheets has four antiparallel strands and has some sequence homology to RNP-1 and RNP-2, which are believed to be RNA-binding motifs and are found in a number of known RNA-binding proteins. Structurally guided mutants may help to uncover the basis for this variety of RNA interaction.

摘要

翻译调节蛋白RegA由T4噬菌体编码,它与信使核糖核酸(mRNA)中包含起始密码子的区域结合。RegA的独特之处在于它能抑制约35种早期T4 mRNA的翻译,但不影响近200种其他mRNA。RegA的晶体结构在1.9埃分辨率下确定;该蛋白质显示具有α螺旋核心和两个带有反平行β折叠的区域。其中一个β折叠有四条反平行链,与RNP - 1和RNP - 2有一些序列同源性,RNP - 1和RNP - 2被认为是RNA结合基序,存在于许多已知的RNA结合蛋白中。结构导向的突变体可能有助于揭示这种多种RNA相互作用的基础。

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