GLYCEROL-3-PHOSPHATE 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。 本论文的研究内容是对大肠杆菌的膜转运蛋白GlpT的结构和转运机制进行研究。GlpT是主要促进剂超家族(MFS)的成员，该家族是最大的次级膜转运蛋白家族，拥有5000多名已知成员。Wanga教授的实验室之前在3.3A分辨率下确定了GlpT的晶体结构。结合结构信息和生化数据，我们提出了底物转运的摇杆开关机制。我的目的是通过测定GlpT与底物的络合物的晶体结构来了解GlpTS底物的特异性和底物诱导的构象变化。我还培养了野生型GlpT的晶体，这种晶体的习性与以前研究中使用的不同。已知这些晶体的冷冻冷却条件(尺寸为100微米x 30微米x 30微米)。人们希望这些晶体将衍射到更高的分辨率，并能够生产出更好的GlpT模型。如果从这些晶体得到的衍射数据足够好，就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.