Department of Physiology and Biophysics, Weill Cornell Medical College, New York, New York, USA.
Nat Struct Mol Biol. 2012 Feb 12;19(3):355-7. doi: 10.1038/nsmb.2233.
We report a structure of a trimeric glutamate transporter homolog from Pyrococcus horikoshii with two protomers in an inward facing state and the third in an intermediate conformation between the outward and inward facing states. The intermediate shows a cavity in the thinnest region of the transporter, which is potentially accessible to extracellular and cytoplasmic solutions. Our findings suggest a structural principle by which transport intermediates may mediate uncoupled permeation of polar solutes.
我们报告了来自 Pyrococcus horikoshii 的三聚体谷氨酸转运蛋白同源物的结构，其中两个原体处于内向构象，第三个处于外向和内向构象之间的中间构象。中间构象显示在转运体最薄的区域有一个腔，该腔可能与细胞外和细胞质溶液相通。我们的发现提出了一个结构原则，即转运中间体能介导极性溶质的不耦合渗透。
