Cheng Yifan
The W.M. Keck Advanced Microscopy Laboratory, Department of Biochemistry and Biophysics, University of California-San Francisco, 600 16th Street, San Francisco, CA 94158, USA.
Curr Opin Struct Biol. 2009 Apr;19(2):203-8. doi: 10.1016/j.sbi.2009.02.004. Epub 2009 Mar 14.
Since the discovery of the 26S proteasome, much progress has been made in determining the structure of this large dynamic protein complex. Until now, a vast amount of structural information of the proteasome has been obtained from all kinds of structure determination techniques, and the function of the protease core is well understood at atomic detail. Yet our understanding of the entire 26S proteasome structure, particularly its 19S regulatory complex, is still limited at a low-resolution blob-ology level. In this review, we highlight the recent progress made in understanding the mechanism of 20S gate opening by the proteasomal activators. We also emphasized the recent methodological advances, particularly in achieving the near atomic resolution by single particle electron cryomicroscopy, and the possible approaches that will enable more detailed structural analysis of the entire 26S proteasome.
自发现26S蛋白酶体以来，在确定这种大型动态蛋白质复合物的结构方面已经取得了很大进展。到目前为止，通过各种结构测定技术已经获得了大量蛋白酶体的结构信息，并且在原子细节上对蛋白酶核心的功能有了很好的理解。然而，我们对整个26S蛋白酶体结构的理解，特别是其19S调节复合物，仍然局限于低分辨率的模糊生物学水平。在这篇综述中，我们重点介绍了在理解蛋白酶体激活剂打开20S门控机制方面取得的最新进展。我们还强调了最近的方法学进展，特别是通过单颗粒电子冷冻显微镜实现近原子分辨率，以及能够对整个26S蛋白酶体进行更详细结构分析的可能方法。
