STRUCTURAL INSIGHT INTO A STAC-LIKE ACTIVE SITE USING A REBC MUTANT

使用 REBC 突变体对类 STAC 活性位点的结构洞察

• 批准号: 8169294
• 负责人: CATHERINE L DRENNAN
• 金额: $ 0.41万
• 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/8169294
• 关键词: Active Sites; Affinity; Anabolism; Binding; Biological Factors; Computer Retrieval of Information on Scientific Projects Database; Enzymes; Funding; Grant; Institution; Mutation; Pathway interactions; Rebeccamycin; Research; Research Personnel; Resources; Source; Staurosporine; Structure; United States National Institutes of Health; insight; mutant

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 enzymes RebC and StaC share a common substrate and 67% homology, yet make different products along separate natural product biosynthetic pathways; RebC and StaC are involved in rebeccamycin and staurosporine biosynthesis, respectively. Their reactivities seem to be regulated by the enzymes' FAD binding affinities. Mutation of key residues in RebC has resulted in a "StaC-like" enzyme in both activity and FAD binding, and we now seek to obtain a crystal structure that might explain these changes.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 RebC 和 StaC 酶具有共同的底物和 67% 的同源性，但沿着不同的天然产物生物合成途径产生不同的产物； RebC 和 StaC 分别参与瑞贝卡霉素和十字孢菌素的生物合成。它们的反应性似乎受到酶的 FAD 结合亲和力的调节。 RebC 中关键残基的突变导致在活性和 FAD 结合方面产生“StaC 样”酶，我们现在寻求获得可能解释这些变化的晶体结构。