6ejk | pdb_00006ejk

Structure of a glycosyltransferase

spinqualitylabelsall models 6ejk, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ejk is a 2 chain structure with sequence from "campylobacter_fetus_subsp._jejuni"_smibert_1974 "campylobacter fetus subsp. jejuni" smibert 1974. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: A2G, BUE, NDG, UDN NonStd Res: MSE Related: 6ejj Gene: wlaC ("Campylobacter fetus subsp. jejuni" Smibert 1974) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 alpha1,4 N-acetylgalactosamine (GalNAc) units to the growing LLO precursor, GalNAc-alpha1,4-GalNAc-alpha1,3-Bac-alpha1-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 facilitating membrane attachment and glycan counting. The ruler helix contains three positively charged side chains that can bind the pyrophosphate group of the LLO substrate and thus limit the addition of GalNAc units to three. These results, combined with molecular dynamics simulations, provide the mechanism of glycan counting by PglH. Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase.,Ramirez AS, Boilevin J, Mehdipour AR, Hummer G, Darbre T, Reymond JL, Locher KP Nat Commun. 2018 Jan 31;9(1):445. doi: 10.1038/s41467-018-02880-2. PMID:29386647 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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