Ontology highlight
ABSTRACT:
SUBMITTER: Liszczak G
PROVIDER: S-EPMC3766382 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
Nature structural & molecular biology 20130804 9
N-terminal acetylation is ubiquitous among eukaryotic proteins and controls a myriad of biological processes. Of the N-terminal acetyltransferases (NATs) that facilitate this cotranslational modification, the heterodimeric NatA complex has the most diversity for substrate selection and modifies the majority of all N-terminally acetylated proteins. Here, we report the X-ray crystal structure of the 100-kDa holo-NatA complex from Schizosaccharomyces pombe, in the absence and presence of a bisubstr ...[more]