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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Crystal structure of heat shock locus V (HslV) from Escherichia coli
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Crystal structure of heat shock locus V (HslV) from Escherichia coli

机译:大肠杆菌的热休克基因座V(HslV)的晶体结构

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摘要

Heat shock locus V (HslV; also called ClpQ) is the proteolytic core of the ATP-dependent protease HslVU in Escherichia coli. It has sequence similarity with the -type subunits of the eukaryotic and archaebacterial proteasomes. Unlike these particles, which display 72-point symmetry, it is a dimer of hexamers with 62-point symmetry. The crystal structure of HslV at 3.8-A deg resolution, determined by isomor- phous replacement and symmetry averaging, shows that in spite of the different symmetry of the particle, the fold and the contacts between subunits are conserved.
机译:热休克基因座V(HslV;也称为ClpQ)是大肠杆菌中ATP依赖性蛋白酶HslVU的蛋白水解核心。它与真核和古细菌蛋白酶体的-型亚基具有序列相似性。与这些粒子显示72点对称性不同,它是具有62点对称性的六聚体的二聚体。通过等构置换和对称平均确定的3.8A deg分辨率下的HslV晶体结构表明,尽管粒子具有不同的对称性,但折叠和亚基之间的接触仍得以保留。

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