来自智人的分子伴侣预折叠蛋白的表达、纯化、结晶及X射线衍射研究。
Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin from Homo sapiens.
作者信息
Aikawa Yoshiki, Kida Hiroshi, Nishitani Yuichi, Miki Kunio
机构信息
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
出版信息
Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1189-93. doi: 10.1107/S2053230X15013990. Epub 2015 Aug 25.
Abstract
Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non-native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non-native actin and tubulin to chaperonin-containing TCP-1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space group P21212, with unit-cell parameters a = 123.2, b = 152.4, c = 105.9 Å.
摘要
正确的蛋白质折叠是所有生物体的一个基本过程。前折叠素（PFD）是一种分子伴侣，它通过将未折叠的蛋白质传递给Ⅱ型伴侣蛋白来协助蛋白质折叠。真核生物PFD的异源六聚体已被证明能特异性识别未折叠的肌动蛋白和微管蛋白，并将其传递给含TCP-1的伴侣蛋白（CCT），但其特异性识别机制仍不清楚。为了确定其晶体结构，重组人PFD被重组、纯化并结晶。收集到了分辨率为4.7 Å的X射线衍射数据。晶体属于空间群P21212，晶胞参数a = 123.2，b = 152.4，c = 105.9 Å。
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