HIGH RESOLUTION CRYSTALLOGRAPHIC STUDIES OF RESPIRATORY PROTEINS FROM T THERMOP

T THERMOP 呼吸蛋白的高分辨率晶体学研究

• 批准号: 7370379
• 负责人: JAMES A FEE
• 金额: $ 0.66万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370379
• 关键词: RESOLUTION; CRYSTALLOGRAPHIC; STUDIES; RESPIRATORY; PROTEINS

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Two proteins, Rieske iron-sulfur and cytochrome ba3, from the thermophilic eubacterium, Thermus thermophilus, involved in respiration are proposed to be studied at high resolution and in multiple oxidation states and pH levels. The oxidized Rieske protein has been solved at pH 8.5 yielding the structure of the partially protonated form, which gives insight into the mechanism of H+ translocation. However, the ultra-high resolution (< 1 ¿¿ structure at pH 8.5, the low pH and reduced state protonated structures at high resolution are also vital to define mechanistic features. Novel ba3 structures of the cyano complex and the reduced, carbonylated form, at high resolution, should yield additional information regarding this protein's function.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子项目和研究者（PI）可能从另一个NIH来源获得主要资金，因此可以在其他CRISP条目中表示。所列机构为中心，不一定是研究者所在机构。建议以高分辨率、多氧化态和pH水平研究来自嗜热真细菌嗜热栖热菌的两种参与呼吸的蛋白质Rieske铁硫和细胞色素ba 3。氧化的Rieske蛋白在pH 8.5下溶解，产生部分质子化形式的结构，这使我们深入了解H+易位的机制。然而，pH 8.5下的超高分辨率（< 1 º）结构、高分辨率下的低pH和还原态质子化结构对于定义机械特征也至关重要。新的ba 3结构的氰基复合物和还原，羰基化的形式，在高分辨率，应该产生额外的信息，关于这种蛋白质的功能。