STRUCTURAL STUDIES OF A BACTERIAL DIVALENT METAL ION TRANSPORTER

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。 二价金属离子转运蛋白(DMT1)是膜转运蛋白中溶质载体(SLC)家族的一员。DMT1蛋白存在于所有生命王国中，根据物种的不同，DMT1蛋白不仅可以运输铁和锰，还可以运输铜、镉和镍等其他微量元素。质子转运是由质子复合体利用膜上的电化学质子梯度来推动的。DMT的结构将提供有关二价金属离子吸收到细胞内的质子驱动运输机制的信息。获得的结构和机制方面的见解将有助于解释与疾病相关的突变，并指导DMT1抑制剂或激活剂的发现。

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. The divalent metal ion transporter (DMT1) is a member of the SoLute Carrier (SLC) group of membrane transport proteins. DMT1 proteins are found in all kingdoms of life and depending on the species transport iron and manganese but also other trace elements like copper, cadmium and nickel. Transport is fueled by proton symport taking advantage of the electrochemical proton gradient across the membrane. The structure of DMT will provide information about the proton- driven transport mechanism of divalent metal ion uptake into cells. The obtained structural and mechanistic insights will help to explain mutations associated with diseases and guide the discovery of DMT1 inhibitors or activators.