NON-HEME IRON HALOGENASES IN NON-RIBOSOMAL PEPTIDE SYNTHESIS (NRPS) PATHWAYS

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 中心，不一定是研究者的机构。 非血红素铁卤化酶被发现作为NRPS系统中的剪裁域。它们属于非血红素铁蛋白的cupin家族，与非血红素铁羟化酶具有惊人的相似性，但它们的反应性非常特异。为了了解非血红素铁卤化酶的反应性，我们已经解决了一个封闭的活性位点和一个开放的活性位点的卤化酶的结构。这些结构的比较有助于我们了解哪些残基对卤化物结合是重要的。 我们还试图解决的第一个结构的非血红素铁羟化酶从NRPS途径，使我们可以直接比较与非血红素铁卤化酶。

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. Non-heme iron halogenases are found as tailoring domains in NRPS systems. They belong to the cupin family of non-heme iron proteins and have striking similarities to non-heme iron hydroxylases yet are very specific in their reactivity. To understand the reactivity of nonheme iron halogenases, we have solved a structure of halogenase with a closed active site and one with an open active site. The comparison of these structures helps us to understand which residues are important for halide binding. We are also attempting to solve the first structure of a nonheme iron hydroxylase from an NRPS pathway so that we can make direct comparisons with the nonheme iron halogenases.