CRYSTAL STRUCTURE OF MOLECULAR CHAPERONE, HSC20

分子伴侣 HSC20 的晶体结构

• 批准号: 6437635
• 负责人: LARRY E VICKERY
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437635
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

Molecular chaperones play key roles in protein folding, transport and across membranes, and in response to stressful stimuli. Hsc20 is a DnaJ-type cochaperone protein encoded in a recently discovered operon in E. coli which encodes a DnaK/hsp70type chaperone. No structure for a DnaJ co-chaperone has been determined although a solution MNR structure of the N-terminal 'Jdomain (100 residues) of DnaJ has revealed secondary structure features.We succeeded in overexpressing, purifying and crystallizing Hsc20. Thus, Hsc20 could provide the first complete high resolution crystal structure for proteins of this class. Diffraction data for the native protein have been obtained to 2.6A using conventional x-ray sources. We prepared two heavy atom derivatives by introducing cysteine residues into protein mutagenesis. Crystals of Hg-labeled crystals are too small to provide data for MIR phasing using our x-ray source, and we seek to determine higher resolution data using the synchrotron radiation source.

分子伴侣在蛋白质折叠，传输中起关键作用 以及跨膜，并响应压力刺激。 HSC20是 在最近发现的 大肠杆菌中的操纵子编码DNAK/HSP70Type伴侣。 不 尽管A 溶液的MNR结构N末端的JDONAR（100个残基） DNAJ揭示了二级结构特征。我们成功地 过表达，净化和结晶HSC20。 因此，HSC20可以 提供第一个完整的高分辨率晶体结构 该类的蛋白质。 天然蛋白的衍射数据 使用常规X射线源获得为2.6a。 我们准备了 通过将半胱氨酸残基引入到 蛋白质诱变。 HG标记晶体的晶体太小 提供用于使用X射线源进行miR逐步逐步逐渐划分的数据，我们试图 使用同步加速器辐射确定更高的分辨率数据 来源。