Toward an atomic model of the 26S proteasome.
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.
Cheng
Yifan
Y
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. ycheng@ucsf.edu
D018360:Crystallography, X-Ray; D004789:Enzyme Activation; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism
D005656:Fungal Proteins; D021122:Protein Subunits; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease