Rigidity of the subunit interfaces of the trimeric glutamate transporter GItT during translocation
Rigidity of the subunit interfaces of the trimeric glutamate transporter GItT during translocation
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DOI：
10.1016/j.jmb.2007.06.067
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发表时间：
2007-09-21
影响因子：
5.6
通讯作者：
Slotboom, Dirk-Jan
中科院分区：
文献类型：
--
作者：
Groeneveld, Maarten;Slotboom, Dirk-Jan
谷氨酸转运蛋白是一种三聚体膜蛋白，其中每个原聚体包含一个单独的转运路径。为了确定转运过程中亚基界面是否发生结构重排，在细菌转运蛋白GltT中引入亚基间二硫键。亚基间的交联，这已经被设计在整个接口，影响谷氨酸转运活性，表明亚基接口是刚性的营业额。
Glutamate transporters are trimeric membrane proteins in which each protomer contains a separate translocation path. To determine whether structural rearrangements take place at the subunit interfaces during transport, intersubunit disulfide bridges were introduced in the bacterial transporter GltT. None of the intersubunit cross-links, which had been designed across the entire interface, affected the glutamate transport activity, indicating that the subunit interfaces are rigid during turnover.