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首页> 外文期刊>Journal of Molecular Biology >Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0
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Structural studies on the oligomeric transition of a small heat shock protein, StHsp14.0

机译：小热激蛋白StHsp14.0的寡聚转变的结构研究

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摘要

The small heat shock proteins (sHsps), which are widely found in all domains of life, bind and stabilize denatured proteins to prevent aggregation. The sHsps exist as large oligomers that are composed of 9-40 subunits and control their chaperone activity by the transition of the oligomeric state. Though the oligomeric transition is important for the biological function of most sHsps, atomic details have not been elucidated. Here, we report crystal structures in both the 24-meric and dimeric states for an sHsp, StHsp14.0 from Sulfolobus tokodaii, in order to reveal changes upon the oligomeric transition. The results indicate that StHsp14.0 forms a spherical 24-mer with a diameter of 115 ?. The diameter is defined by the inter-monomer angle in the dimer. The dimer structure in the dimeric state shows only small differences from that in the 24-meric state. Some significant differences are exclusively observed at the binding site for the C-terminus. Although a dimer has four interactive sites with neighboring dimers, the weakness of the respective interactions is indicated from the size-exclusion chromatography. The small structural changes imply an activation mechanism mediated by multiple weak interactions.
机译：在生活的所有领域中广泛发现的小型热激蛋白（sHsps）结合并稳定变性蛋白以防止聚集。 sHsps作为大型低聚物存在，由9-40个亚基组成，并通过低聚状态的转变控制其分子伴侣活性。尽管低聚转变对于大多数sHsps的生物学功能很重要，但原子的细节尚未阐明。在这里，我们报道了来自Sulfolobus tokodaii的sHsp，StHsp14.0的24位和二位状态的晶体结构，以揭示寡聚转变时的变化。结果表明StHsp14.0形成直径为115Ω的球形24聚体。该直径由二聚体中的单体间角定义。二聚体状态下的二聚体结构与24聚体状态下仅显示出很小的差异。仅在C末端的结合位点观察到一些显着差异。尽管二聚体具有四个与相邻二聚体相互作用的位点，但是从尺寸排阻色谱法表明了各自相互作用的弱点。小的结构变化暗示了由多个弱相互作用介导的激活机制。

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