Ontology highlight
ABSTRACT:
SUBMITTER: Pathare GR
PROVIDER: S-EPMC3939901 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Pathare Ganesh Ramnath GR Nagy István I Śledź Paweł P Anderson Daniel J DJ Zhou Han-Jie HJ Pardon Els E Steyaert Jan J Förster Friedrich F Bracher Andreas A Baumeister Wolfgang W
Proceedings of the National Academy of Sciences of the United States of America 20140210 8
The ATP-dependent degradation of polyubiquitylated proteins by the 26S proteasome is essential for the maintenance of proteome stability and the regulation of a plethora of cellular processes. Degradation of substrates is preceded by the removal of polyubiquitin moieties through the isopeptidase activity of the subunit Rpn11. Here we describe three crystal structures of the heterodimer of the Mpr1-Pad1-N-terminal domains of Rpn8 and Rpn11, crystallized as a fusion protein in complex with a nanob ...[more]