CRYSTALLOGRAPHY OF PROLINE CATABOLIC ENZYMES, PHOSPHATASES, AND PARVALBUMINS

脯氨酸分解酶、磷酸酶和小清蛋白的晶体学

• 批准号: 8169278
• 负责人: JOHN J TANNER
• 金额: $ 0.7万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169278
• 关键词: Acid Phosphatase; Affinity; Apoptosis; Bacteria; Binding; Birds; Buffers; Calcium; Calcium-Binding Proteins; Catabolism; Complex; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Data; Disease; EF Hand Motifs; Electrons; Enzymes; Funding; Generations; Glutamates; Goals; Grant; Histidine; Inborn Genetic Diseases; Institution; Length; Malignant Neoplasms; Metal Ion Binding; Metals; Oxidation-Reduction; Oxidoreductase; Parvalbumins; Phosphoric Monoester Hydrolases; Play; Proline; Proline Dehydrogenase; Rattus; Research; Research Personnel; Resolution; Resources; Role; Source; Structure; Substrate Specificity; Superoxides; System; United States National Institutes of Health; Water; X ray diffraction analysis; X-Ray Diffraction; analog; avian thymic hormone; base; carboxylate; oxidation; phosphomonoester; protein function; pyrroline

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. The goal of this project is determine crystal structures of proline catabolic enzymes, phosphatases, and parvalbumins. The proline catabolic enzymes proline dehydrogenase (PRODH) and pyrroline-5-carboxylate dehydrogenase (P5CDH) catalyze the 4-electron oxidation of proline to glutamate. These enzymes play important roles in cellular redox control, superoxide generation, apoptosis, and cancer. Inborn errors of proline catabolism result in hyperprolinemia disorders Type I (PRODH) and Type II (P5CDH). In some bacteria, the two enzymes are fused into the bifunctional enzyme, proline utilization A (PutA). PutAs thus serve as systems for studying substrate channeling. The goal of part of the project is to collect high resolution single crystal X-ray diffraction data for several proline catabolic enzymes, including monofunctional PRODH and P5CDH enzymes, PutA domains, and full-length PutAs. Phosphatases catalyze the transfer of a phosphoryl group from phosphomonoesters to water. Phosphatases under study include histidine acid phosphatases (HAPs) and class C acid phosphatases (CCAPs). Our main goal is to determine crystal structures of these phosphatases complexed with substrates and substrate analogues to elucidate the basis for substrate specificity. Parvalbumins (PVs) are small EF-hand calcium-binding proteins that function mainly in calcium buffering. The goal of this part of the project is to elucidate the structural basis for the different metal ion-binding signatures of three representative parvalbumins that span a wide range of metal binding affinity: avian thymic hormone (ATH) and rat beta-PV and avian parvalbumin 3.

这个子项目是众多研究子项目之一