Rigidity of the subunit interfaces of the trimeric glutamate transporter GItT during translocation

被引:54
作者
Groeneveld, Maarten [1 ]
Slotboom, Dirk-Jan [1 ]
机构
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Biochem, NL-9747 AG Groningen, Netherlands
关键词
membrane protein; glutamate transport; oligomeric state; transport mechanism; subunit interaction;
D O I
10.1016/j.jmb.2007.06.067
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:565 / 570
页数:6
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