Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase from Campylobacter jejuni.

Glycobiology - 1 Oct 2017

Barre Yasmin, Nothaft Harald, Thomas Cody, Liu Xin, Li Jianjun, Ng Kenneth K S, Szymanski Christine M

Abstract excerpt

In Campylobacter jejuni, the PglB oligosaccharyltransferase catalyzes the transfer of a heptasaccharide from a lipid donor to asparagine within the D/E-X1-N-X2-S/T sequon (X1,2 ≠ P) or releases this heptasaccharide as free oligosaccharides (fOS). Using available crystal structures and sequence alignments, we identified a DGGK motif near the active site of PglB that is conserved among all Campylobacter species. We...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Proteins
Share to Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Campylobacter jejuni

Share to Conserved Sequence

Share to Glycosyltransferases

Share to Lipopolysaccharides

Share to Molecular Docking Simulation

Share to Polysaccharides

Source

Identifiers

PMID: 28922740
DOI: 10.1093/glycob/cwx067

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A conserved DGGK motif is essential for the function of the PglB oligosaccharyltransferase from Campylobacter jejuni.PMID 28922740Read ↗

Identifying the targets and functions of N -linked protein glycosylation in Campylobacter jejuniSemantic proximity Read ↗

A catalytically essential motif in external loop 5 of the bacterial oligosaccharyltransferase PglB.Semantic proximity Read ↗

Functional analysis of the Campylobacter jejuni N-linked protein glycosylation pathway.Semantic proximity Read ↗

Characterization of the structurally diverse N-linked glycans of Campylobacter species.Semantic proximity Read ↗

Study of free oligosaccharides derived from the bacterial N-glycosylation pathway.Semantic proximity Read ↗

Biosynthesis of the N-linked glycan in Campylobacter jejuni and addition onto protein through block transfer.Semantic proximity Read ↗

Increased efficiency of Campylobacter jejuni N-oligosaccharyltransferase PglB by structure-guided engineering.Semantic proximity Read ↗

The ALPK1 pathway drives the inflammatory response to Campylobacter jejuni in human intestinal epithelial cellsSemantic proximity Read ↗

Modification of the Campylobacter jejuni N-Linked Glycan by EptC Protein-mediated Addition of PhosphoethanolamineSemantic proximity Read ↗

The crucial role of Campylobacter jejuni genes in anti-ganglioside antibody induction in Guillain-Barre syndrome.Semantic proximity Read ↗

Comparative genomics analysis of completely sequenced microbial genomes reveals the ubiquity of N-linked glycosylation in prokaryotes.Semantic proximity Read ↗

N-linked glycosylation in Campylobacter jejuni and its functional transfer into E. coli.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.