EC Number   |
|---|
   3.4.25.1 | - |
| 3.4.25.1 | cryo-EM structures of the actively ATP-hydrolyzing, substrate-engaged 26S proteasome with four distinct motor conformations. Structures suggest a ubiquitin capture mechanism, in which mechanical pulling on the substrate by the AAA+ motor delivers ubiquitin modifications directly into the Rpn11 catalytic groove and accelerates isopeptide cleavage for efficient, cotranslocational deubiquitination. The substrate polypeptide traverses from the Rpn11 deubiquitinase, through the AAA+ motor, and into the core peptidase. The proteasomal motor thereby adopts staircase arrangements with five substrate-engaged subunits and one disengaged subunit. Four of the substrate-engaged subunits are ATP bound, whereas the subunit at the bottom of the staircase and the disengaged subunit are bound to ADP |
| 3.4.25.1 | crystal structure of the enzyme in complex with the competitive inhibitor acetyl-Leu-Leu-norleucinal |
| 3.4.25.1 | enzyme core particle with the alpha7DELTAN mutation, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.5), 50 mM magnesium acetate, and 14% (v/v) 2-methyl-2,4-pentanediol |
| 3.4.25.1 | hanging drop vapour diffusion method, structure of the 20S proteasome/TMC-95A complex |
| 3.4.25.1 | in complex with bortezomib, hanging drop vapour diffusion method at 24°C in 30 mM MgOAc, 100 mM MES (pH 7.2), and 10% 2-methyl-2,4-pentanediol |
| 3.4.25.1 | in complex with carfilzomib, hanging drop vapor diffusion method, using 0.2 M sodium formate, 40% (w/v) 2-methyl-2,4-pentanediol, at 16°C |
| 3.4.25.1 | in complex with peptide KYFTGSKLWRSYYA, to 3 A resolution |
| 3.4.25.1 | purified 20S protease core, X-ray diffraction structure determination and analysis |
| 3.4.25.1 | single particle cryo-electron microscoppy |
