CRYSTALLOGRAPHIC STUDIES OF METALLOENZYMES

金属酶的晶体学研究

• 批准号: 7370699
• 负责人: JESSICA VEY
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-03-01 至 2007-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7370699
• 关键词: CRYSTALLOGRAPHIC; STUDIES; METALLOENZYMES

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 intend to gain rapid access time to continue our studies of SAM Radical enzymes and non-heme mononuclear iron proteins. We hope to add to our understanding of formation and control of the 5'-deoxyadenosyl radical by SAM Radical enzymes for reaction with highly diverse substrates. We are also interested in SyrB2, a non-heme mononuclear iron protein which catalyzes a chloride insertion reaction without precedent in biology. Our rapid access time will be used to solve the first structures of Pyruvate-formate lyase activase, one of the best biochemically characterized SAM Radical enzymes, as well as SyrB2, which also has not yet been structurally characterized.

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。我们打算获得快速访问时间，以继续我们对SAM自由基酶和非血红素单核铁蛋白的研究。我们希望加深我们对SAM自由基酶对5‘-脱氧腺苷自由基的形成和控制的了解，以便于与高度多样化的底物反应。我们还对SyrB2感兴趣，这是一种非血红素单核铁蛋白，它催化氯离子插入反应，在生物学上没有先例。我们的快速访问时间将用于解决丙酮酸-甲酸裂解酶激活酶的第一个结构，丙酮酸-甲酸裂解酶是生化特征最好的SAM自由基酶之一，以及SyrB2，它也尚未被结构表征。