Conformational switching of the 26S proteasome enables substrate degradation

被引：0

作者：

Mary E Matyskiela

Gabriel C Lander

Andreas Martin

机构：

[1] University of California,Department of Molecular and Cell Biology

[2] Berkeley,Life Sciences Division

[3] Lawrence Berkeley National Laboratory,undefined

[4] University of California,undefined

[5] Berkeley,undefined

[6] California Institute for Quantitative Biosciences,undefined

[7] University of California,undefined

[8] Berkeley,undefined

[9] Present address: Scripps Research Institute,undefined

[10] La Jolla,undefined

[11] California,undefined

[12] USA.,undefined

来源：

Nature Structural & Molecular Biology | 2013年 / 20卷

关键词：

D O I：

暂无

中图分类号：

学科分类号：

摘要：

The proteasome 19S particle processes ubiquitinated substrates, unfolds the polypeptides and translocates them to the 20S core particle. Now cryo-EM analyses of the yeast proteasome in the presence of substrate show the 19S in an active conformation, with the AAA+ ring forming a wider central channel aligned with the 20S pore and the essential deubiquitinase Rpn11 positioned right above it.

引用

页码：781 / 788

页数：7

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