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-Structure paper
タイトル | A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年1月9日 |
著者 | Zev A Ripstein / Siavash Vahidi / Walid A Houry / John L Rubinstein / Lewis E Kay / |
PubMed 要旨 | The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ...The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins. ClpXP is an important target for drug development against infectious diseases. Although structures are available for isolated ClpX and ClpP rings, it remains unknown how symmetry mismatched ClpX and ClpP work in tandem for processive substrate translocation into the ClpP proteolytic chamber. Here, we present cryo-EM structures of the substrate-bound ClpXP complex from at 2.3 to 3.3 Å resolution. The structures allow development of a model in which the sequential hydrolysis of ATP is coupled to motions of ClpX loops that lead to directional substrate translocation and ClpX rotation relative to ClpP. Our data add to the growing body of evidence that AAA+ molecular machines generate translocating forces by a common mechanism. |
リンク | Elife / PubMed:31916936 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.3 - 4.1 Å |
構造データ | EMDB-21187, PDB-6vfs: EMDB-21194, PDB-6vfx: EMDB-21195: EMDB-21196: |
化合物 | ChemComp-ATP: ChemComp-MG: ChemComp-ADP: |
由来 |
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キーワード | HYDROLASE / Complex / AAA+ / protease / ClpP / ClpX |