STRUCTURE OF A MYCOBACTERIAL PHOSPHORIBOSE EPIMERASE

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来源获得了主要资金， 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。 磷酸核糖差向异构酶产生合成分枝杆菌独特的细菌细胞壁的关键中间体。由于它们在这组细菌中的独特功能，它们代表了开发抗结核分枝杆菌新药的有吸引力的靶点。然而，目前还没有蛋白质的结构，以帮助在这方面的努力，开发新的小分子抑制剂对这些enzymes.We最近已经能够获得这样的磷酸核糖差向异构酶的衍射晶体。初步的X射线衍射实验表明，结构的解决方案，使用硒代甲硫氨酸衍生物将是可行的，只要可以收集到更高的分辨率数据。

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.