Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.

ABSTRACT: The membrane-associated, processive and retaining glycosyltransferase PglH from Campylobacter jejuni is part of the biosynthetic pathway of the lipid-linked oligosaccharide (LLO) that serves as the glycan donor in bacterial protein N-glycosylation. Using an unknown counting mechanism, PglH catalyzes the transfer of exactly three α1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-α1,4-GalNAc-α1,3-Bac-α1-PP-undecaprenyl. Here, we present crystal structures of PglH in three distinct states, including a binary complex with UDP-GalNAc and two ternary complexes containing a chemo-enzymatically generated LLO analog and either UDP or synthetic, nonhydrolyzable UDP-CH₂-GalNAc. PglH contains an amphipathic helix ("ruler helix") that has a dual role of facilitat

SUBMITTER: Ramirez AS 

PROVIDER: S-EPMC5792488 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature