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Structure and mechanism of a na+-independent amino Acid transporter

handsomeland 添加于 2009-8-22 18:18 | 2568 次阅读 | 0 个评论

作者
Shaffer PL, Goehring A, Shankaranarayanan A, Gouaux E
摘要
Amino acid, polyamine, and organocation (APC) transporters are secondary transporters that play essential roles in nutrient uptake, neurotransmitter recycling, ionic homeostasis, and regulation of cell volume. Here, we present the crystal structure of apo-ApcT, a proton-coupled broad-specificity amino acid transporter, at 2.35 angstrom resolution. The structure contains 12 transmembrane helices, with the first 10 consisting of an inverted structural repeat of 5 transmembrane helices like the leucine transporter LeuT. The ApcT structure reveals an inward-facing, apo state and an amine moiety of lysine-158 located in a position equivalent to the sodium ion site Na2 of LeuT. We propose that lysine-158 is central to proton-coupled transport and that the amine group serves the same functional role as the Na2 ion in LeuT, thus demonstrating common principles among proton- and sodium-coupled transporters.
详细资料
- 文献种类:期刊
- 期刊名称: Science (New York, N.Y.)
- 期刊缩写: Science
- 期卷页: 2009年第325卷第5943期 1010-1014页
- 地址: Vollum Institute, Oregon Health and Science University, 3181 Southwest Sam Jackson Park Road, Portland, OR 97239, USA
- ISBN: 1095-9203
标签

氨基酸转运体结构神经传导
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