DIFFRACTION DATA COLLECTION FROM PROTEIN CRYSTALS

蛋白质晶体的衍射数据收集

• 批准号: 8170614
• 负责人: JAMES F PARSONS
• 金额: $ 0.54万
• 依托单位: BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-07-01 至 2011-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170614
• 关键词: Acids; Anabolism; Antibiotics; Biochemical; Chemistry; Coenzyme A; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Data Collection; Development; Environment; Erwinia; Funding; Grant; Human; Infection; Institution; Ligase; Organism; Pantoea agglomerans; Phenazines; Physical condensation; Proteins; Reaction; Research; Research Personnel; Resources; Source; Structure; System; Therapeutic; United States National Institutes of Health; Work; antimicrobial; design; interest; killings; microorganism; research study

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. D-alanylgriseoluteic acid (AGA) is a broad spectrum antibiotic produced by Pantoea agglomerans (aka Erwinia herbicola), an enterobacterial species that is known to produce a number of interesting antimicrobial compounds. P. agglomerans appears to deploy AGA to kill other microorganisms in its local environment thus enhancing its competitiveness. AGA has been shown particularly effective against gram positive organisms. Certain strains of P. agglomerans are also capable of causing serious infections in humans. Thus we are interested not only in the chemistry of AGA biosynthesis from the standpoint of assessing the development of AGA like molecules as therapeutics. Many of the other steps in AGA biosynthesis are uncharacterized or poorly characterized. The subject of this work EhpF appears to be a phenazine CoA ligase that, we speculate, activates a phenazine substrate for a condensation reaction that modifies the phenazine ring system. Determination of the structure of EhpF will permit a comparison with other CoA liagses and will facilitate the design of specific biochemical experiments.

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 D-丙氨酰灰解酸(AGA)是一种广谱抗生素，由聚集性泛细菌(又名草本欧文氏菌)产生，是一种肠道细菌，能产生许多有趣的抗菌化合物。聚集性巴氏杆菌似乎利用AGA杀死其本地环境中的其他微生物，从而增强其竞争力。AGA已被证明对革兰氏阳性菌特别有效。聚集性巴氏杆菌的某些菌株也能在人类中引起严重感染。因此，我们不仅从评估AGA类分子作为治疗药物的发展的角度出发，对AGA生物合成的化学感兴趣。AGA生物合成中的许多其他步骤都没有特征或特征不佳。这项工作的主题EhpF似乎是吩嗪CoA连接酶，我们推测，它激活吩嗪底物进行缩合反应，从而改变吩嗪环系统。确定EhpF的结构将允许与其他CoA实验进行比较，并将有助于设计特定的生化实验。