Chiba Institute of Science, Choshi, Chiba, 288-0025, Japan.
Anticancer Res. 2009 Nov;29(11):4897-900.
The ADP/ATP carrier catalyzes the exchange of ADP and ATP across the inner mitochondrial membrane.
The molecular dynamics of modeled yeast type 2 AAC (yAAC2) was analyzed and molecular parameters were determined.
The yAAC2 C-terminal moved flexibly and a negative electrostatic potential field (ESP) was located in the C-terminal region. The ESP field is always located in the C-terminal area during C-terminal truncation (d1-d9). Further C-terminal truncation occurred on field invagination into the core region (d11, d14, d16). The 2-6 C-terminal amino acid truncation did not affect the biological activity. The d7-d9 truncated mutants lost their biological function.
A critical point in yAAC2 function was shown between d6 and d7 C-terminal truncation. The C-terminal structure of yAAC2 is thought to be involved in biological function control.
ADP/ATP 载体催化 ADP 和 ATP 在线粒体内膜之间的交换。
分析了模型酵母 2 型 AAC(yAAC2)的分子动力学,并确定了分子参数。
yAAC2 的 C 末端可灵活移动,C 末端区域存在负静电势能场(ESP)。在 C 末端截断(d1-d9)过程中,ESP 场始终位于 C 末端区域。进一步的 C 末端截断发生在 ESP 场向内核区域凹陷(d11、d14、d16)。2-6 个 C 末端氨基酸截断不影响生物活性。d7-d9 截断的突变体失去了其生物功能。
yAAC2 功能的关键点显示在 d6 和 d7 个 C 末端截断之间。yAAC2 的 C 末端结构被认为参与了生物功能的控制。