STRUCTURE STUDIES OF MOLECULAR CHAPERON HEAT SHOCK PROTEIN 40(HSP 40)

热休克蛋白70（Hsp 7 O）家族的分子伴侣 结合未折叠的多肽底物以稳定或改变它们的 构象并水解ATP以促进多肽释放。 的 Hsp 70的ATP水解受另一种蛋白伴侣的调节 热休克蛋白40（Hsp 4 O）（1）. 据报 Hsp 4 O可以结合具有二级结构的多肽， 直接与Hsp 70结合，刺激Hsp 70的ATP水解。 热休克蛋白4 O 它本身也可以结合变性的多肽，并将它们重新折叠成 独立蛋白伴侣（2）。 Sis I是Hsp 4 O蛋白的一个成员 家族在酵母酿酒酵母中，它是细胞所必需的 生存力（3）。 我们最近已经结晶了蛋白质Sis I， 晶体在SSRL站7- 1处被激发到2.7A。 我们建议解决 在BioCARS Station 14上用MAD方法测定SiI的晶体结构 BM-D

Molecular chaperones of the Heat Shock Protein 70(Hsp7O) family bind unfolded polypeptide substrates to stabilize or alter their conformation and hydrolyze ATP to facilitate polypeptide release. The ATP hydrolysis of Hsp70 is regulated by another protein chaperon family Heat Shock Protein 40(Hsp4O)(1). It has been reported that Hsp4O may bind polypeptides with secondary structure, interact directly with Hsp70 and stimulate the ATP hydrolysis of Hsp70. Hsp4O itself can also bind denatured polypeptides and refold them as an independent protein chaperone(2). Sis I is a member of Hsp4O protein family in yeast Saccharomyces cerevisiae and it is essential for cell viability(3). We have crystallized the protein Sis I recently, the crystals diffract to 2.7A at SSRL station 7- 1. We propose to solve the crystal structure of Sis I by MAD method on BioCARS Station 14 BM-D.