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、运输中起着关键作用