New crystal structure of proteasome-dedicated chaperone Rpnl4 at 1.6 Å resolution.
New crystal structure of proteasome-dedicated chaperone Rpnl4 at 1.6 Å resolution.
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蛋白酶体专用分子伴侣 Rpnl4 的新晶体结构，分辨率为 1.6 Å。
DOI：
10.1107/s1744309112011359
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
T.
中科院分区：
文献类型：
--
作者：
Kim;S.;Nishide;A.;Saeki;Y.;Takagi;K.;Tanaka;K.;Kato;K.;Mizushima;T.
26 S蛋白酶体是一种ATP依赖性蛋白酶，负责选择性降解多聚泛素化蛋白。最近的研究表明，蛋白酶体组装是一个高度有序的多步骤过程，由特定的分子伴侣辅助。Rpn 14是ATP酶环形成的组装分子伴侣，特异性识别ATP酶亚基Rpt 6。Rpn 14在2.0 nm分辨率下的结构在空间群P64中先前已被报道，但Rpn 14功能的详细机制仍不清楚。 在这里，一个新的晶体结构的Rpn 14与E384 A突变的空间群P21在1.6 <$m分辨率。 这种高分辨率的结构为理解蛋白酶体组装提供了一个框架。
The 26S proteasome is an ATP-dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi-step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase-ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 Å resolution in space group P64 has previously been reported, but the detailed mechanism of Rpn14 function remains unclear. Here, a new crystal structure of Rpn14 with an E384A mutation is presented in space group P21 at 1.6 Å resolution. This high-resolution structure provides a framework for understanding proteasome assembly.