Aikawa Yoshiki, Kida Hiroshi, Nishitani Yuichi, Miki Kunio
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1189-93. doi: 10.1107/S2053230X15013990. Epub 2015 Aug 25.
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.
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。
