2Z5E

Crystal Structure of Proteasome Assembling Chaperone 3

Summary for 2Z5E

• Entry DOI: 10.2210/pdb2z5e/pdb
• Descriptor: Proteasome Assembling Chaperone 3 (2 entities in total)
• Functional Keywords: beta sandwich, homodimer, proteasome, chaperone
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 26236.88

Authors

Okamoto, K.,Kurimoto, E.,Sakata, E.,Suzuki, A.,Yamane, T.,Hirano, Y.,Murata, S.,Tanaka, K.,Kato, K. (deposition date: 2007-07-06, release date: 2008-02-19, 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

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

Experimental method

X-RAY DIFFRACTION (2 Å)