TERTIARY AND QUATERNARY STRUCTURE CHARACTERIZATION OF METALLOENZYMES IN SOLUTION

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。列出的机构是 中心，不一定是研究者的机构。 MtrA是来自细菌希瓦氏菌（Shewanella oneidensis）的10-血红素细胞色素。这种蛋白质还没有晶体结构。最近提出的一个假说表明，它是一种高度不对称的蛋白质，纵横比约为4：1，这将允许血红素平行堆叠。用SAXS测定其回转半径和低分辨率溶液结构将使我们能够研究这一假设，并进一步了解这种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.