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: 7954159
• 负责人: JAMES A FEE
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954159
• 关键词: Complex; Computer Retrieval of Information on Scientific Projects Database; Eubacterium; Funding; Grant; Institution; Proteins; Research; Research Personnel; Resolution; Resources; Respiration; Rieske iron-sulfur protein; Source; Structure; Thermus thermophilus; United States National Institutes of Health; cytochrome ba3; insight; novel; oxidation; protein function; respiratory protein; structural biology; synchrotron radiation; ultra high resolution

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 ba(3), 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 ba(3) structures of the cyano complex and the reduced, carbonylated form, at high resolution, should yield additional information regarding this protein's function.

该副本是使用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这是调查员的机构。 提议在高分辨率和多种氧化态和pH水平下研究两种蛋白质，rieske铁硫和细菌的rieske rieske rieske rieske Iron-Sulfur和细胞色素Ba（3）。氧化的Rieske蛋白已在pH 8.5下求解，得出部分质子化形式的结构，从而深入了解H（+）易位的机理。但是，在pH 8.5时，超高分辨率（<1€）结构，高分辨率下的低pH和降低态质子化结构对于确定的机械特征也至关重要。新型BA（3）Cyano复合物的结构和降低的羰基形式在高分辨率下应产生有关该蛋白质功能的其他信息。