Vardy Eyal, Arkin Isaiah T, Gottschalk Kay E, Kaback H Ronald, Schuldiner Shimon
Alexander Silberman Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem, 91904 Israel.
Protein Sci. 2004 Jul;13(7):1832-40. doi: 10.1110/ps.04657704.
The structures of membrane transporters are still mostly unsolved. Only recently, the first two high-resolution structures of transporters of the major facilitator superfamily (MFS) were published. Despite the low sequence similarity of the two proteins involved, lactose permease and glycerol-3-phosphate transporter, the reported structures are highly similar. This leads to the hypothesis that all members of the MFS share a similar structure, regardless of their low sequence identity. To test this hypothesis, we generated models of two other members of the MFS, the Tn10-encoded metal-tetracycline/H(+) antiporter (TetAB) and the rat vesicular monoamine transporter (rVMAT2). The models are based on the two MFS structures and on experimental data. The models for both proteins are in good agreement with the data available and support the notion of a shared fold for all MFS proteins.
膜转运蛋白的结构大多仍未得到解析。直到最近，主要易化子超家族（MFS）转运蛋白的前两个高分辨率结构才得以发表。尽管所涉及的两种蛋白质，即乳糖通透酶和甘油 - 3 - 磷酸转运蛋白，其序列相似性较低，但报道的结构却高度相似。这引发了一个假设，即MFS的所有成员都共享相似的结构，无论它们的序列同一性有多低。为了验证这一假设，我们构建了MFS的另外两个成员的模型，即Tn10编码的金属 - 四环素/H(+)反向转运蛋白（TetAB）和大鼠囊泡单胺转运蛋白（rVMAT2）。这些模型基于两个MFS结构以及实验数据。这两种蛋白质的模型与现有数据高度吻合，并支持所有MFS蛋白质具有共享折叠的观点。
