Department of Biochemistry, University of Groningen, Groningen Biomolecular Science and Biotechnology Institute, Nijenborgh 4, 9747 AG Groningen, The Netherlands.
Biochemistry. 2010 May 4;49(17):3511-3. doi: 10.1021/bi100430s.
The Na(+) aspartate symporter Glt(Ph) from Pyrococcus horikoshii is the only member of the glutamate transporter family for which crystal structures have been determined. The cation:aspartate coupling stoichiometry is unknown, thus hampering the elucidation of the ion coupling mechanism. Here we measure transport of (22)Na(+) and [(14)C]aspartate in proteoliposomes containing purified Glt(Ph) and demonstrate that three Na(+) ions are symported with aspartate.
来自 Pyrococcus horikoshii 的 Na(+) 天冬氨酸协同转运蛋白 Glt(Ph) 是唯一一种已确定晶体结构的谷氨酸转运蛋白家族成员。阳离子:天冬氨酸偶联计量比未知,从而阻碍了离子偶联机制的阐明。在这里,我们在含有纯化的 Glt(Ph) 的脂质体中测量 (22)Na(+) 和 [(14)C]天冬氨酸的转运,并证明三个 Na(+) 离子与天冬氨酸协同转运。