Signal Transduction in Nitrogenase Fe Protein

固氮酶 Fe 蛋白的信号转导

• 批准号: 7480328
• 负责人: Michael Alan Vance
• 金额: $ 4.68万
• 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/7480328
• 关键词: Affect; Amino Acids; Binding; Biochemical; Biological Models; Calorimetry; Cell physiology; Class; Complex; Computational Technique; Crystallography; Electron Transport; Environment; Goals; Hormones; Hydrolysis; Knowledge; Learning; Metabolic; MgATP; Modeling; Molecular Biology; Muscle Contraction; Nitrogenase; Nucleotides; Potential Energy; Process; Property; Protein Biosynthesis; Proteins; Quantum Mechanics; Roentgen Rays; Role; Signal Transduction; Solutions; Standards of Weights and Measures; Structure; Surface; System; Techniques; Variant; X-Ray Crystallography; analog; insight; member; molecular mechanics; mutant; nitrogenase reductase; nucleoside triphosphate; physical property; post-doctoral training; protein structure

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（由申请人提供）：信号转导，多种细胞过程（例如蛋白质生物合成、激素刺激的代谢活动、肌肉收缩等）中的重要机制，部分是通过由三磷酸核苷结合和水解诱导的蛋白质构象变化来进行的。固氮酶中的Fe蛋白就是这类蛋白的一员。虽然存在固氮酶组分蛋白的结构，但影响构象变化和MgATP水解的因素还不清楚。该提案的主要目标是使用生物化学、生物物理学和计算技术（X射线晶体学、小角X射线散射、量热法和QM/MM计算）来定义Fe蛋白在核苷酸结合、水解和信号转导过程中的构象变化以及氨基酸环境对调节[4Fe-4S]簇性质的影响。