GLYCEROL-3-PHOSPHATE TRANSPORTER

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 研究中心，而研究中心不一定是研究者所在的机构。 本论文的主要研究内容是对大肠杆菌膜转运蛋白GlpT的结构和转运机制的研究。杆菌GlpT是主要易化因子超家族（MFS）的成员，MFS是最大的二级膜转运蛋白家族，已知有超过5000个成员。Wanga教授的实验室先前以3.3 A的分辨率确定了GlpT的晶体结构。结合结构信息与生化数据，我们提出了一个摇杆开关机制的基板运输。我的目的是了解GlpT底物特异性和底物诱导的构象变化，通过确定GlpT的晶体结构与底物的复合物。我还生长了野生型GlpT的晶体，其习性与以前的研究中使用的晶体不同。对于这些晶体（其尺寸为100 μ m × 30 μ m × 30 μ m），低温冷却条件是已知的。人们希望这些晶体能够达到更高的分辨率，并能够产生更好的GlpT模型。如果从这些晶体得到的衍射数据足够好，则可以通过分子置换来确定结构。

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. My research involves studying the structure and transport mechanism of the integral membrane transporter protein, GlpT, the glycerol-3-phosphate (G3P) transporter from E. coli. GlpT is a member of the major facilitator superfamily (MFS), the largest secondary membrane transporter family, with over 5000 known members. Prof. Wanga's lab previously determined the crystal structure of GlpT at 3.3 A resolution. Combining the structural information with biochemical data, we proposed a rocker-switch mechanism for substrate transport. I aim to understand GlpTs substrate specificity and substrate-induced conformational change by determining the crystal structure of GlpT in complex with a substrate. I have also grown crystals of wild-type GlpT that differ in habit from those used in previous studies. Cryo-cooling conditions are known for these crystals (which measure 100 um x 30 um x 30 um). It is hoped these crystals will diffract to a higher resolution and enable a better model of GlpT to be produced. If the diffraction data that derives from these crystals is good enough, the structure can be determined by molecular replacement.