3VL1

Crystal structure of yeast Rpn14

Summary for 3VL1

• Entry DOI: 10.2210/pdb3vl1/pdb
• Related: 3ACP
• Descriptor: 26S proteasome regulatory subunit RPN14 (2 entities in total)
• Functional Keywords: beta-propeller, chaperone, rpt6
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Cytoplasm: P53196
• Total number of polymer chains: 2
• Total formula weight: 93315.85

Authors

Kim, S.,Nishide, A.,Saeki, Y.,Takagi, K.,Tanaka, K.,Kato, K.,Mizushima, T. (deposition date: 2011-11-28, release date: 2012-05-02, Last modification date: 2023-11-08)

Primary citation

Kim, S.,Nishide, A.,Saeki, Y.,Takagi, K.,Tanaka, K.,Kato, K.,Mizushima, T.
New crystal structure of the proteasome-dedicated chaperone Rpn14 at 1.6 A resolution
Acta Crystallogr.,Sect.F, 68:517-521, 2012

PubMed Abstract: The 26S proteasome is an ATP-dependent protease responsible for selective degradation of polyubiquitylated proteins. Recent studies have suggested that proteasome assembly is a highly ordered multi-step process assisted by specific chaperones. Rpn14, an assembly chaperone for ATPase-ring formation, specifically recognizes the ATPase subunit Rpt6. The structure of Rpn14 at 2.0 Å resolution in space group P6(4) has previously been reported, but the detailed mechanism of Rpn14 function remains unclear. Here, a new crystal structure of Rpn14 with an E384A mutation is presented in space group P2(1) at 1.6 Å resolution. This high-resolution structure provides a framework for understanding proteasome assembly.

PubMed: 22691779
DOI: 10.1107/S1744309112011359

Experimental method

X-RAY DIFFRACTION (1.6 Å)