2Z5B
Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly
Summary for 2Z5B
Entry DOI | 10.2210/pdb2z5b/pdb |
Related | 2Z5C |
Descriptor | Protein YPL144W, Uncharacterized protein YLR021W (3 entities in total) |
Functional Keywords | proteasome, chaperone, s. cerevisiae |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Cytoplasm: Q12245 |
Total number of polymer chains | 2 |
Total formula weight | 36957.10 |
Authors | Yashiroda, H.,Mizushima, T.,Okamoto, K.,Kameyama, T.,Hayashi, H.,Kishimoto, T.,Kasahara, M.,Kurimoto, E.,Sakata, E.,Suzuki, A.,Hirano, Y.,Murata, S.,Kato, K.,Yamane, T.,Tanaka, K. (deposition date: 2007-07-03, release date: 2008-01-22, Last modification date: 2024-03-13) |
Primary citation | Yashiroda, H.,Mizushima, T.,Okamoto, K.,Kameyama, T.,Hayashi, H.,Kishimoto, T.,Niwa, S.,Kasahara, M.,Kurimoto, E.,Sakata, E.,Takagi, K.,Suzuki, A.,Hirano, Y.,Murata, S.,Kato, K.,Yamane, T.,Tanaka, K. Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes Nat.Struct.Mol.Biol., 15:228-236, 2008 Cited by PubMed Abstract: Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled. PubMed: 18278057DOI: 10.1038/nsmb.1386 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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