PROTEIN CRYSTAL STRUCTURE DETERMINATIONS RELATED TO NITRIC OXIDE SIGNALING AND O

与一氧化氮信号传导和 O 相关的蛋白质晶体结构测定

• 批准号: 8170151
• 负责人: SUE L ROBERTS
• 金额: $ 0.37万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170151
• 关键词: Bacteria; Binding; Collaborations; Computer Retrieval of Information on Scientific Projects Database; Evolution; Funding; GTP Cyclohydrolase; Glutathione; Grant; Heme; Hemeproteins; Homeostasis; Institution; Maps; Metal Binding Site; Metals; Nitric Oxide; Nitrosation; Oxidoreductase; Proteins; Research; Research Personnel; Resolution; Resources; Riboflavin; Signal Transduction; Signaling Protein; Site; Soluble Guanylate Cyclase; Source; Structure; Time; United States National Institutes of Health; base; drug discovery; synchrotron radiation

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. We request beam time to further several projects. First, we are studying nitrosylated heme proteins, including nitrophorins and heme-based NO signaling proteins, particularly soluble guanylate cyclase (sGC). Second, we are continuing studies of protein S-nitrosation, and control of glutathione S-nitrosation by the protein GSNO reductase. The GSNOR studies include a drug discovery component. Third, we are investigating proteins involved in riboflavin synthesis, particularly the GTP cyclohydrolases. Fourth, we are expanding studies of proteins involved in metal transport and homeostasis in bacteria, focusing on cusF, silF, cusB, and cueO. Finally, we will, in collaboration with Matt Cordes, use structure determinations guided by transitive homology studies to map fold evolution of Cro proteins and lipocalins. Crystals are available for all projects. Some diffract to 1.0 ¿ or better. Synchrotron radiation is needed for (1) MAD structure determination, (2) to provide sufficient resolution to determine accurate geometrical parameters such as heme distortion from planarity and metal binding site geometries; (3) to provide variable wavelength x-rays for unambiguous identification of bound metal atoms and to control photoreduction of metal sites and S-NO bonds.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中央赠款提供的资源 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此，在列出的机构中可能会被压制 对于中心，这不一定是调查员的工厂。 我们要求Beam Tirther几个项目。 - 蛋白质还原酶的硝基化。 Lipocalins。或者，（1）MAD结构确定需要更高的同步辐射，以确定准确的几何街机（例如平面性和金属结合位点几何形状）的精确几何划分；金属位点和S-NO键。