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。 非血红素铁卤化酶在NRPS系统中被发现是剪裁结构域。它们属于非血红素铁蛋白的Cupin家族，与非血红素铁羟基酶有着惊人的相似之处，但它们的反应活性却非常特异。为了了解非血红素铁卤化酶的反应活性，我们解决了卤化酶的一个封闭活性中心和一个开放活性中心的结构。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。我们还试图从NRPS途径中解出非血红素铁羟基酶的第一个结构，以便我们可以直接与非血红素铁卤化酶进行比较。

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.