Ontology highlight
ABSTRACT:
SUBMITTER: Menyhard DK
PROVIDER: S-EPMC3682586 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
The Journal of biological chemistry 20130430 24
Oligopeptidases impose a size limitation on their substrates, the mechanism of which has long been under debate. Here we present the structure of a hexameric serine protease, an oligopeptidase from Pyrococcus horikoshii (PhAAP), revealing a complex, self-compartmentalized inner space, where substrates may access the monomer active sites passing through a double-gated "check-in" system, first passing through a pore on the hexamer surface and then turning to enter through an even smaller opening a ...[more]