CRYSTAL-STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA-COLI
CRYSTAL-STRUCTURE OF CSPA, THE MAJOR COLD SHOCK PROTEIN OF ESCHERICHIA-COLI
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DOI：
10.1073/pnas.91.11.5119
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发表时间：
1994-05-24
影响因子：
11.1
通讯作者：
HEINEMANN, U
中科院分区：
文献类型：
--
作者：
SCHINDELIN, H;JIANG, WN;HEINEMANN, U
大肠杆菌的主要冷休克蛋白CspA是在生长温度快速下降时产生的，它参与至少两个基因的转录调控。该蛋白与Y-box因子的核酸结合域具有高度同源性，Y-box因子是一个参与转录和翻译调节的真核蛋白家族。在2埃分辨率下测定了CspA的晶体结构，并将其细化为R = 0.187。CspA由五条反平行的β链组成，形成一个封闭的五链β桶。CspA的三维结构与枯草芽孢杆菌（Bacillus subtilis）的主要冷休克蛋白CspB相似，CspB最近被确定为2.45埃的分辨率。然而，与CspB相反，晶体中没有形成二聚体。CspA的表面是蛋白质与单链核酸相互作用的特征。由于细菌冷休克蛋白与Y-box因子的高度同源性，大肠杆菌CspA和枯草芽孢杆菌CspB定义了普通冷休克域的结构框架。
The major cold shock protein of Escherichia coli, CspA, produced upon a rapid downshift in growth temperature, is involved in the transcriptional regulation of at least two genes. The protein shares high homology with the nucleic acid-binding domain of the Y-box factors, a family of eukaryotic proteins involved in transcriptional and translational regulation. The crystal structure of CspA has been determined at 2-Angstrom resolution and refined to R = 0.187. CspA is composed of five antiparallel beta-strands forming a closed five-stranded beta-barrel. The three-dimensional structure of CspA is similar to that of the major cold shock protein of Bacillus subtilis, CspB, which has recently been determined at 2.45-Angstrom resolution. However, in contrast to CspB, no dimer is formed in the crystal. The surface of CspA is characteristic for a protein interacting with single-stranded nucleic acids. Due to the high homology of the bacterial cold shock proteins with the Y-box factors, E. coli CspA and B. subtilis CspB define a structural framework for the common cold shock domain.