Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications
复制标题
DOI：
10.1006/jsbi.1997.3954
复制
发表时间：
1998-01-01
影响因子：
3
通讯作者：
Mannella, CA
中科院分区：
文献类型：
--
作者：
Mannella, CA
电压依赖性阴离子选择性通道（VDAC）通常被认为是代谢物跨线粒体外膜扩散的主要途径。它还与多种线粒体和胞浆蛋白相互作用，包括激酶和细胞色素 c。序列分析和圆二色性表明该通道是细菌孔蛋白样β-桶，然而，与细菌孔蛋白不同，VDAC不会形成紧密的三聚体复合物，并且很容易被膜电位和低pH值门控（可逆关闭）。圆二色性表明蛋白质在 pH 值下发生了主要的构象变化
The voltage-dependent, anion-selective channel (VDAC) is generally considered the main pathway for metabolite diffusion across the mitochondrial outer membrane. It also interacts with several mitochondrial and cytosolic proteins, including kinases and cytochrome c. Sequence analysis and circular dichroism suggest that the channel is a bacterial porin-like beta-barrel, However, unlike bacterial porins, VDAC does not form tight trimeric complexes and is easily gated (reversibly closed) by membrane potential and low pH. Circular dichroism indicates that the protein undergoes a major conformational change at pH