3WHJ

Crystal structure of Nas2 N-terminal domain

Summary for 3WHJ

• Entry DOI: 10.2210/pdb3whj/pdb
• Related: 2DZN 3ACP 3H4M 3VLD 3VLE 3VLF 3WHK 3WHL
• Descriptor: Probable 26S proteasome regulatory subunit p27, SULFATE ION, CADMIUM ION, ... (4 entities in total)
• Functional Keywords: proteasome assembly chaperone, chaperone
• Biological source: Saccharomyces cerevisiae (yeast)
• Total number of polymer chains: 1
• Total formula weight: 14615.90

Authors

Satoh, T.,Saeki, Y.,Hiromoto, T.,Wang, Y.-H.,Uekusa, Y.,Yagi, H.,Yoshihara, H.,Yagi-Utsumi, M.,Mizushima, T.,Tanaka, K.,Kato, K. (deposition date: 2013-08-26, release date: 2014-03-26, Last modification date: 2024-05-29)

Primary citation

Satoh, T.,Saeki, Y.,Hiromoto, T.,Wang, Y.H.,Uekusa, Y.,Yagi, H.,Yoshihara, H.,Yagi-Utsumi, M.,Mizushima, T.,Tanaka, K.,Kato, K.
Structural basis for proteasome formation controlled by an assembly chaperone nas2.
Structure, 22:731-743, 2014

PubMed Abstract: Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.

PubMed: 24685148
DOI: 10.1016/j.str.2014.02.014

Experimental method

X-RAY DIFFRACTION (1.65 Å)