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的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 酶RebC和StaC共享共同的底物和67%的同源性，但沿着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了活性和FAD结合的“StaC样”酶，我们现在寻求获得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.