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

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。 RebC和Stac酶具有相同的底物和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星形孢子素的生物合成。它们的反应活性似乎受到酶的FAD结合亲和力的调节。RebC关键残基的突变导致了活性和FAD结合方面的“Stc样”酶，我们现在寻求获得一种可能解释这些变化的晶体结构。

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.