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-Structure paper
タイトル | Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases. |
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ジャーナル・号・ページ | Mol Cell, Vol. 30, Issue 3, Page 360-368, Year 2008 |
掲載日 | 2008年5月9日 |
著者 | Julius Rabl / David M Smith / Yadong Yu / Shih-Chung Chang / Alfred L Goldberg / Yifan Cheng / |
PubMed 要旨 | Substrates enter the cylindrical 20S proteasome through a gated channel that is regulated by the ATPases in the 19S regulatory particle in eukaryotes or the homologous PAN ATPase complex in archaea. ...Substrates enter the cylindrical 20S proteasome through a gated channel that is regulated by the ATPases in the 19S regulatory particle in eukaryotes or the homologous PAN ATPase complex in archaea. These ATPases contain a conserved C-terminal hydrophobic-tyrosine-X (HbYX) motif that triggers gate opening upon ATP binding. Using cryo-electron microscopy, we identified the sites in the archaeal 20S where PAN's C-terminal residues bind and determined the structures of the gate in its closed and open forms. Peptides containing the HbYX motif bind to 20S in the pockets between neighboring alpha subunits where they interact with conserved residues required for gate opening. This interaction induces a rotation in the alpha subunits and displacement of a reverse-turn loop that stabilizes the open-gate conformation. This mechanism differs from that of PA26/28, which lacks the HbYX motif and does not cause alpha subunit rotation. These findings demonstrated how the ATPases' C termini function to facilitate substrate entry. |
リンク | Mol Cell / PubMed:18471981 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 6.8 Å |
構造データ | |
由来 |
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キーワード | HYDROLASE / protein peptide complex / peptide not modeled. / Protease / Proteasome / Threonine protease / protein complex |