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
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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.
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页码：781 / 788
页数：7
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