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: 7954493
• 负责人: SUE L ROBERTS
• 金额: $ 0.06万
• 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/7954493
• 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; structural biology; 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。 我们要求光束时间进一步进行几个项目。首先，我们正在研究亚硝基化的血红素蛋白，包括硝基磷酸蛋白和基于血红素的无信号蛋白，尤其是可溶性鸟苷酸环化酶（SGC）。其次，我们正在继续研究蛋白S-硝化作用，并通过蛋白质GSNO还原酶控制谷胱甘肽S-硝化。 GSNOR研究包括药物发现成分。第三，我们正在研究参与核黄素合成的蛋白质，尤其是GTP环氢酶。第四，我们正在扩大对细菌中金属运输和稳态涉及的蛋白质的研究，重点是CUSF，SILF，CUSB和CUEO。最后，我们将与Matt Cordes合作，使用以及时同源性研究为指导的结构确定来绘制CRO蛋白和Lipocalins的折叠演化。晶体可用于所有项目。有些衍射为1.0或更好。 （1）MAD结构确定需要同步辐射，（2）提供足够的分辨率来确定准确的几何参数，例如平面性和金属结合位点几何形状的血红素失真； （3）提供可变的波长X射线，以明确鉴定结合金属原子并控制金属位点和S-NO键的光doinugion。