The Structure of the Mammalian 20S Proteasome at 2.75 Å Resolution

• Published in: Structure (London) Vol. 10; no. 5; pp. 609 - 618
• Main Authors: Unno, Masaki, Mizushima, Tsunehiro, Morimoto, Yukio, Tomisugi, Yoshikazu, Tanaka, Keiji, Yasuoka, Noritake, Tsukihara, Tomitake
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.05.2002
• Subjects: 20S proteasome; Animals; Binding Sites; Cattle; crystal structure analysis; Crystallography, X-Ray; Cysteine Endopeptidases - chemistry; Cysteine Endopeptidases - genetics; Humans; immunoproteasome; Liver - enzymology; mammalian proteasome; Models, Molecular; Molecular Structure; Multienzyme Complexes - chemistry; Multienzyme Complexes - genetics; Ntn-hydrolase; Proteasome Endopeptidase Complex; Protein Conformation; Protein Structure, Tertiary; Protein Subunits; structure organization; Substrate Specificity; crystal structure analysis; Ntn-hydrolase; immunoproteasome; 20S proteasome; structure organization; mammalian proteasome
• ISSN: 0969-2126; 1878-4186
• DOI: 10.1016/S0969-2126(02)00748-7

The 20S proteasome is the catalytic portion of the 26S proteasome. Constitutively expressed mammalian 20S proteasomes have three active subunits, β1, β2, and β5, which are replaced in the immunoproteasome by interferon-γ-inducible subunits β1i, β2i, and β5i, respectively. Here we determined the crystal structure of the bovine 20S proteasome at 2.75 Å resolution. The structures of α2, β1, β5, β6, and β7 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 β7 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.