Ontology highlight
ABSTRACT:
SUBMITTER: Ozcelik D
PROVIDER: S-EPMC4351746 | biostudies-literature | 2012
REPOSITORIES: biostudies-literature
Nature communications 20120101
Pupylation is a posttranslational protein modification occurring in mycobacteria and other actinobacteria that is functionally analogous to ubiquitination. Here we report the crystal structures of the modification enzymes involved in this pathway, the prokaryotic ubiquitin-like protein (Pup) ligase PafA and the depupylase/deamidase Dop. Both feature a larger amino-terminal domain consisting of a central β-sheet packed against a cluster of helices, a fold characteristic for carboxylate-amine liga ...[more]