Structure of bacterial oligosaccharyltransferase PglB bound to a reactive LLO and an inhibitory peptide.

ABSTRACT: Oligosaccharyltransferase (OST) is a key enzyme of the N-glycosylation pathway, where it catalyzes the transfer of a glycan from a lipid-linked oligosaccharide (LLO) to an acceptor asparagine within the conserved sequon N-X-T/S. A previous structure of a ternary complex of bacterial single subunit OST, PglB, bound to a non-hydrolyzable LLO analog and a wild type acceptor peptide showed how both substrates bind and how an external loop (EL5) of the enzyme provided specific substrate-binding contacts. However, there was a relatively large separation of the substrates at the active site. Here we present the X-ray structure of PglB bound to a reactive LLO analog and an inhibitory peptide, revealing previously unobserved interactions in the active site. We found that the atoms forming the N-gly

SUBMITTER: Napiorkowska M 

PROVIDER: S-EPMC6215017 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature