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2Z5B

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

2Z5B の概要
エントリーDOI10.2210/pdb2z5b/pdb
関連するPDBエントリー2Z5C
分子名称Protein YPL144W, Uncharacterized protein YLR021W (3 entities in total)
機能のキーワードproteasome, chaperone, s. cerevisiae
由来する生物種Saccharomyces cerevisiae (baker's yeast)
詳細
細胞内の位置Cytoplasm: Q12245
タンパク質・核酸の鎖数2
化学式量合計36957.10
構造登録者
主引用文献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: 18278057
DOI: 10.1038/nsmb.1386
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.96 Å)
構造検証レポート
Validation report summary of 2z5b
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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