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2Z5B

Crystal Structure of a Novel Chaperone Complex for Yeast 20S Proteasome Assembly

Summary for 2Z5B
Entry DOI10.2210/pdb2z5b/pdb
Related2Z5C
DescriptorProtein YPL144W, Uncharacterized protein YLR021W (3 entities in total)
Functional Keywordsproteasome, chaperone, s. cerevisiae
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Cellular locationCytoplasm: Q12245
Total number of polymer chains2
Total formula weight36957.10
Authors
Primary citationYashiroda, 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: 18278057
DOI: 10.1038/nsmb.1386
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.96 Å)
Structure validation

229380

數據於2024-12-25公開中

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