Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0
Dimer structure and conformational variability in the N-terminal region of an archaeal small heat shock protein, StHsp14.0
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DOI：
10.1016/j.jsb.2010.12.006
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发表时间：
2011-04-01
影响因子：
3
通讯作者：
Miki, Kunio
中科院分区：
文献类型：
--
作者：
Takeda, Kazuki;Hayashi, Takuro;Miki, Kunio
小热休克蛋白 (sHsps) 属于一类分子伴侣，可结合并稳定变性蛋白质以防止聚集。小热激蛋白在不同的寡聚状态之间进行转变以控制其疏水性。迄今为止，仅报道了大寡聚状态的sHsps的结构。在这里，我们报道了来自 Sulfolobus tokodaii 的二聚体状态的 StHsp14.0 的结构，它是通过 C 端 IXI/V 基序的突变形成的。二聚体是两种晶体形式的唯一组成部分，二聚体模式与大寡聚体中的相同。 N-末端螺旋的构象多种多样。此外，还进行了光谱和生化实验来研究 N 末端的构象变异性。结构、动力学和寡聚体特性表明 StHsp14.0 的伴侣活性是由部分溶解的寡聚体介导的。 (C) 2011 Elsevier Inc. 保留所有权利。
Small heat shock proteins (sHsps), which are categorized into a class of molecular chaperones, bind and stabilize denatured proteins to prevent aggregation. The sHsps undergo transition between different oligomeric states to control their hydrophobicity. So far, only the structures of sHsps in large oligomeric states have been reported. Here we report the structure of StHsp14.0 from Sulfolobus tokodaii in the dimeric state, which is formed by means of a mutation at the C-terminal IXI/V motif. The dimer is the sole building block in two crystal forms, and the dimeric mode is the same as that in the large oligomers. The N-terminal helix has variety in its conformation. Furthermore, spectroscopic and biochemical experiments were performed to investigate the conformational variability at the N-terminus. The structural, dynamical and oligomeric properties suggest that chaperone activity of StHsp14.0 is mediated by partially dissolved oligomers. (C) 2011 Elsevier Inc. All rights reserved.