STRUCTURE OF A MYCOBACTERIAL PHOSPHORIBOSE EPIMERASE

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。 磷酸核糖差向异构酶是合成分枝杆菌独特细菌细胞壁的关键中间体。由于它们在这类细菌中的独特功能，它们是开发抗结核分枝杆菌新药的有吸引力的靶点。然而，目前还没有蛋白质结构来帮助开发针对这些酶的新的小分子抑制剂。我们最近能够获得一种这样的磷酸核糖异构体酶的衍射晶。初步的X射线衍射实验表明，一旦收集到更高分辨率的数据，使用硒蛋氨酸衍生物的结构溶液将是可行的。

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. Phosphoribose epimerases produce key intermediates for the synthesis of the unique bacterial cell wall of mycobacteria. Because of their unique function in this group of bacteria, they represent attractive targets for the development of new drugs against Mycobacterium tuberculosis. However, there are no protein structures currently available to aid in this effort to develop new small molecule inhibitors against these enzymes.We have recently been able to obtain diffracting crystals for one such phosphoribose epimerase. Preliminary X-ray diffraction experiments show that a structure solution using selenomethionine derivatives will be feasible as soon as higher resolution data can be collected.