Ontology highlight
ABSTRACT:
SUBMITTER: Baek K
PROVIDER: S-EPMC7050210 | biostudies-literature | 2020 Feb
REPOSITORIES: biostudies-literature
Baek Kheewoong K Krist David T DT Prabu J Rajan JR Hill Spencer S Klügel Maren M Neumaier Lisa-Marie LM von Gronau Susanne S Kleiger Gary G Schulman Brenda A BA
Nature 20200212 7795
Eukaryotic cell biology depends on cullin-RING E3 ligase (CRL)-catalysed protein ubiquitylation<sup>1</sup>, which is tightly controlled by the modification of cullin with the ubiquitin-like protein NEDD8<sup>2-6</sup>. However, how CRLs catalyse ubiquitylation, and the basis of NEDD8 activation, remain unknown. Here we report the cryo-electron microscopy structure of a chemically trapped complex that represents the ubiquitylation intermediate, in which the neddylated CRL1<sup>β-TRCP</sup> promo ...[more]