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Literature summary for 3.4.25.1 extracted from

  • de la Pena, A.H.; Goodall, E.A.; Gates, S.N.; Lander, G.C.; Martin, A.
    Substrate-engaged 26S proteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation (2018), Science, 362, 6418 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P21243
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Scl1
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Saccharomyces cerevisiae