A gated channel into the proteasome core particle
A gated channel into the proteasome core particle
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DOI：
10.1038/80992
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发表时间：
2000-11-01
期刊：
影响因子：
--
通讯作者：
Finley, D
中科院分区：
文献类型：
--
作者：
Groll, M;Bajorek, M;Finley, D
酵母蛋白酶体的核心颗粒（CP）是由四个七聚体环的亚基排列在一个中空的，桶状结构。我们报告说，CP是自动抑制的N-末端尾部的外（α）环亚基。晶体学分析表明，α 3-亚基的尾部的缺失打开了一个通道进入CP的蛋白水解活性内室，从而解抑制肽水解。在粒子的潜伏状态下，尾部通过对CP施加拓扑闭合来防止衬底进入。当调节颗粒与CP结合形成蛋白酶体全酶时，α-亚基尾部的抑制被解除。
The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the a-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.