1IRU

Crystal Structure of the mammalian 20S proteasome at 2.75 A resolution

1IRU の概要

• エントリーDOI: 10.2210/pdb1iru/pdb
• 分子名称: 20S proteasome, MAGNESIUM ION, ... (16 entities in total)
• 機能のキーワード: 20s proteasome, cell cycle, immune response, proteolysis, ubiquitin, hydrolase
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Cytoplasm: P33672
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 718069.73

構造登録者

Unno, M.,Mizushima, T.,Morimoto, Y.,Tomisugi, Y.,Tanaka, K.,Yasuoka, N.,Tsukihara, T. (登録日: 2001-10-24, 公開日: 2002-05-22, 最終更新日: 2024-11-06)

主引用文献

Unno, M.,Mizushima, T.,Morimoto, Y.,Tomisugi, Y.,Tanaka, K.,Yasuoka, N.,Tsukihara, T.
The structure of the mammalian 20S proteasome at 2.75 A resolution.
Structure, 10:609-618, 2002

PubMed Abstract: The 20S proteasome is the catalytic portion of the 26S proteasome. Constitutively expressed mammalian 20S proteasomes have three active subunits, beta 1, beta 2, and beta 5, which are replaced in the immunoproteasome by interferon-gamma-inducible subunits beta 1i, beta 2i, and beta 5i, respectively. Here we determined the crystal structure of the bovine 20S proteasome at 2.75 A resolution. The structures of alpha 2, beta 1, beta 5, beta 6, and beta 7 subunits of the bovine enzyme were different from the yeast enzyme but enabled the bovine proteasome to accommodate either the constitutive or the inducible subunits. A novel N-terminal nucleophile hydrolase activity was proposed for the beta 7 subunit. We also determined the site of the nuclear localization signals in the molecule. A model of the immunoproteasome was predicted from this constitutive structure.

PubMed: 12015144
DOI: 10.1016/S0969-2126(02)00748-7

実験手法

X-RAY DIFFRACTION (2.75 Å)