TERTIARY AND QUATERNARY STRUCTURE CHARACTERIZATION OF METALLOENZYMES IN SOLUTION

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。 MTRA是一种含有10个血红素的细胞色素，由单氏希瓦氏菌产生。这种蛋白质目前还不存在晶体结构。最近提出的一种假说认为，它是一种高度不对称的蛋白质，长宽比约为4：1，这将允许血红素平行堆积。用SAXS确定其旋转半径和低分辨溶液结构将使我们能够研究这一假说，并进一步了解该蛋白质中的电子转移机制。

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. MtrA is a 10-heme cytochrome from the bacteria, Shewanella oneidensis. No crystal structure yet exists for this protein. A recently proposed hypothesis suggests that it is a highly asymmetric protein with an aspect ratio of ~ 4:1, which would allow parallel stacking of the hemes. Determination of its radius of gyration and low-resolution solution structure with SAXS will allow us to investigate this hypothesis and further understand the mechanism of electron transfer in this protein.