3ACP
Crystal Structure of Yeast Rpn14, a Chaperone of the 19S Regulatory Particle of the Proteasome
Summary for 3ACP
| Entry DOI | 10.2210/pdb3acp/pdb |
| Descriptor | WD repeat-containing protein YGL004C (2 entities in total) |
| Functional Keywords | wd40 domain, wd repeat, chaperone |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Cytoplasm: P53196 |
| Total number of polymer chains | 1 |
| Total formula weight | 46433.68 |
| Authors | Kim, S.,Saeki, Y.,Suzuki, A.,Takagi, K.,Fukunaga, K.,Yamane, T.,Kato, K.,Tanaka, K.,Mizushima, T. (deposition date: 2010-01-08, release date: 2010-03-16, Last modification date: 2011-07-13) |
| Primary citation | Kim, S.,Saeki, Y.,Fukunaga, K.,Suzuki, A.,Takagi, K.,Yamane, T.,Tanaka, K.,Mizushima, T.,Kato, K. Crystal structure of yeast Rpn14, a chaperone of the 19S regulatory particle of the proteasome J.Biol.Chem., 285:15159-15166, 2010 Cited by PubMed Abstract: The ubiquitin-proteasome pathway is a major proteolytic system in eukaryotic cells and regulates various cellular processes. The 26 S proteasome, the central enzyme of this pathway, consists of a proteolytic core particle and two 19 S regulatory particles (RPs) composed of ATPase (Rpt) and non-ATPase (Rpn) subunits. Growing evidence indicates that proteasome assembly is assisted by a variety of chaperones. In particular, it has been reported recently that Nas2, Nas6, Rpn14, and Hsm3 bind specific Rpt subunits, thereby contributing to the formation of 19 S RP. Rpn14 transiently binds to the C-terminal domain of the Rpt6 subunit (Rpt6-C) during maturation of the ATPase ring of 19 S RP. In this study, we determined the crystal structure of yeast Rpn14 at 2.0 A resolution, which revealed that this chaperone consists of a unique N-terminal domain with unknown function and a C-terminal domain assuming a canonical seven-bladed beta-propeller fold. The Rpt6-binding site on Rpn14 was predicted based on structural comparison with the complex formed between Nas6 and Rpt3-C. The top face of Rpn14 exhibits a highly acidic surface area, whereas the putative interacting surface of Rpt6-C is basic. By inspection of structural data along with genetic and biochemical data, we determined the specific residues of Rpn14 and Rpt6 for complementary charge interactions that are required for 19 S RP assembly. PubMed: 20236927DOI: 10.1074/jbc.M110.104042 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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