MULTIWAVELENGTH ANOMALOUS DISPERSION DATA COLLECTION FROM E COLI FABH CRYSTALS

从大肠杆菌 FABH 晶体中收集多波长反常色散数据

• 批准号: 6667830
• 负责人: STEPHEN W WHITE
• 金额: $ 14.27万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-09-30 至 2003-08-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6667830
• 关键词: bioimaging /biomedical imaging; biological products; biomedical resource; proteins; radiography; structural biology

We propose to determine the structure of a complex between the E. coli chaperonin GroEL (Cpn60) and the gp 5 capsid protein of bacteriophage HK97. Suitable crystals have been obtained, they can be flash frozen at -160oC and preliminary data have been collected at CHESS to 3.6
resolution. Chaperonins, including members of the Cpn60 family are a ubiuitous class of proteins that assist in protein folding in vivo by binding to partially folded proteins; this prevents aggregation and may unfold off pathway intermediates and direct them back into the correct folding pathway. The gp 5 protein is a natural substrate of GroEL; it is the major capsid protein in the ocosahedral head of the lambdoid bacteriophage HK97. The unit cell parameters are: a = 138.0,b = 270.9, c = 155.4
, b = 101.4o. The Space Group is P2. The asymmetric unit contains one 14mer of GroEL and one subunit of the HK97 gp5 protein, i.e. it is the smallest asymmetric unti that could contain a complete complex of this type.

我们建议确定E. 大肠杆菌伴侣蛋白GroEL（Cpn 60）和大肠杆菌gp 5衣壳蛋白 噬菌体HK 97。 已经获得了合适的晶体，它们可以是 在-160 ℃下快速冷冻，并在 国际象棋3.6
分辨率 监护人，包括 Cpn 60家族是一类普遍存在的蛋白质， 通过结合部分折叠的蛋白质在体内折叠;这防止了 聚集，并可能展开的途径中间体，并指导他们 回到正确的折叠路径。 gp 5蛋白是一种天然的 GroEL的底物;它是八面体中的主要衣壳蛋白 噬菌体HK 97的头部。 晶胞参数 结果为：a = 138.0，b = 270.9，c = 155.4
，B = 101.4o。 空间群 是P2。 不对称单元含有一个GroEL的14聚体和一个GroEL的14聚体。 它是HK 97 gp 5蛋白的最小的不对称亚基，即它是HK 97 gp 5蛋白的最小的不对称亚基。 直到它可能包含这种类型的完整复合体。