Structural insights into ABC transporter mechanism.
Structural insights into ABC transporter mechanism.
复制标题
DOI：
10.1016/j.sbi.2008.09.007
复制
发表时间：
2008-12
影响因子：
6.8
通讯作者：
Chen, Jue
中科院分区：
文献类型：
--
作者：
Oldham, Michael L.;Davidson, Amy L.;Chen, Jue
ATP结合盒（ABC）转运蛋白利用来自ATP水解的能量到整个膜上的物质。近年来，几种ABC转运蛋白的晶体结构已获得。这些结构表明，进口商和出口商均在两个构象之间振荡：与底物易位途径的向内构象，向细胞质开放，以及与面向膜相对侧的易位途径的外向构象。在这篇综述中，分析了同源ABC转运蛋白结构中发现的构象差异，以了解如何实现交替访问。看来，跨膜亚基的刚体旋转与核苷酸结合亚基的开口和闭合相吻合，夫妻ATP水解为底物易位。
ATP-binding cassette (ABC) transporters utilize the energy from ATP hydrolysis to transport substances across the membrane. In recent years, crystal structures of several ABC transporters have become available. These structures show that both importers and exporters oscillate between two conformations: an inward-facing conformation with the substrate translocation pathway open to the cytoplasm and an outward-facing conformation with the translocation pathway facing the opposite side of the membrane. In this review, conformational differences found in the structures of homologous ABC transporters are analyzed to understand how alternating-access is achieved. It appears that rigid-body rotations of the transmembrane subunits, coinciding with the opening and closing of the nucleotide-binding subunits, couples ATP hydrolysis to substrate translocation.
登录
查看更多内容
影响因子：
3.2
作者：
Ehrle, R;Pick, C;Ehrmann, M
通讯作者：
Ehrmann, M
影响因子：
56.9
作者：
Locher, KP;Lee, AT;Rees, DC
通讯作者：
Rees, DC
影响因子：
64.8
作者：
Oldham, Michael L.;Khare, Dheeraj;Chen, Jue
通讯作者：
Chen, Jue
影响因子：
64.8
作者：
Hollenstein, Kaspar;Frei, Dominik C.;Locher, Kaspar P.
通讯作者：
Locher, Kaspar P.
影响因子：
3.2
作者：
TREPTOW, NA;SHUMAN, HA
通讯作者：
SHUMAN, HA