Signal Transduction in Nitrogenase Fe Protein

固氮酶 Fe 蛋白的信号转导

• 批准号: 7157679
• 负责人: Michael Alan Vance
• 金额: $ 4.4万
• 依托单位: MONTANA STATE UNIVERSITY - BOZEMAN
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-08-01 至 2009-07-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7157679
• 关键词: X ray crystallography; adenosine triphosphate; aminoacid; bioenergetics; biological signal transduction; calorimetry; conformation; enzyme complex; enzyme mechanism; hemoprotein; hydrolysis; low angle X ray diffraction analysis; magnesium; mutant; nitrogenase; nucleotides; postdoctoral investigator; quantum chemistry

DESCRIPTION (provided by applicant): Signal transduction, an important mechanism in a variety of cellular processes (e.g. protein biosynthesis, hormone stimulated metabolic activities, muscle contraction, etc.), is carried out in part through protein conformational changes induced by nucleoside triphosphate binding and hydrolysis. The Fe protein in nitrogenase is one member of this class of proteins. Although structures exist for nitrogenase component proteins, the factors affecting conformational change and MgATP hydrolysis are not well understood. The major objectives of this proposal are to use biochemical, biophysical, and computational techniques (x- ray crystallography, small angle x-ray scattering, calorimetry, and QM/MM calculations) to define conformational changes in the Fe protein during nucleotide binding, hydrolysis, and signal transduction as well as effects of amino acid environment on modulating [4Fe-4S] cluster properties.

描述(申请人提供)：信号转导是多种细胞过程(如蛋白质生物合成、激素刺激的代谢活动、肌肉收缩等)中的重要机制，部分通过核苷三磷酸结合和水解引起的蛋白质构象变化来进行。固氮酶中的铁蛋白是这类蛋白中的一员。虽然固氮酶组成蛋白的结构存在，但影响构象变化和镁ATP水解的因素还不是很清楚。这个建议的主要目标是使用生化、生物物理和计算技术(X射线结晶学、小角X射线散射、量热和QM/MM计算)来确定核苷酸结合、水解和信号转导过程中铁蛋白的构象变化，以及氨基酸环境对调节[4Fe-4S]簇属性的影响。