首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of Vibrio cholerae ribosome hibernation promoting factor
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Structure of Vibrio cholerae ribosome hibernation promoting factor

机译:霍乱弧菌核糖体冬眠促进因子的结构

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The X-ray crystal structure of ribosome hibernation promoting factor (HPF) from Vibrio cholerae is presented at 2.0 angstrom resolution. The crystal was phased by two-wavelength MAD using cocrystallized cobalt. The asymmetric unit contained two molecules of HPF linked by four Co atoms. The metal-binding sites observed in the crystal are probably not related to biological function. The structure of HPF has a typical fold consistent with previous structures of YfiA and HPF from Escherichia coli. Comparison of the new structure with that of HPF from E. coli bound to the Thermus thermophilus ribosome [Polikanov et al. (2012), Science, 336, 915918] shows that no significant structural changes are induced in HPF by binding.
机译:霍乱弧菌核糖体冬眠促进因子(HPF)的X射线晶体结构的分辨率为2.0埃。使用共结晶的钴通过两波长MAD对晶体进行定相。不对称单元包含两个由四个Co原子连接的HPF分子。晶体中观察到的金属结合位点可能与生物学功能无关。 HPF的结构具有典型的折叠,该折叠与大肠杆菌的YfiA和HPF的先前结构一致。新结构与结合到嗜热栖热菌核糖体的大肠杆菌中HPF的比较[Polikanov等。 (2012),Science,336,915918]显示通过结合在HPF中没有诱导出明显的结构变化。

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