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Asparagine-linked protein glycosylation: from eukaryotic to prokaryotic systems.
TLDR
A detailed comparison of the machinery involved in the N-linked glycosylation systems of eukaryotic organisms, exemplified by the yeast Saccharomyces cerevisiae, with that of the bacterial system in C. jejuni is provided.
The expanding horizons of asparagine-linked glycosylation.
TLDR
Recent progress toward gaining a deeper biochemical understanding of this modification across all three kingdoms will be summarized and a brief overview of the role of N-linked glycosylation in viruses will also be presented.
At the membrane frontier: a prospectus on the remarkable evolutionary conservation of polyprenols and polyprenyl-phosphates.
TLDR
This review surveys the available research to explore why unmodified polyprenols have been conserved in evolution and whypolyprenyl-phosphates are universally and specifically utilized for membrane-bound glycan assembly.
In vitro biosynthesis of UDP-N,N'-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system.
TLDR
It is found that the UDP-4-amino-sugar was readily synthesized from UDP-GlcNAc in a coupled reaction using PglF and PglE and the structure determined by NMR analysis.
Dynamic and specific interaction between synaptic NR2-NMDA receptor and PDZ proteins
TLDR
Analysis of dynamic interaction between NR2 C termini and proteins containing PSD-95/Discs-large/ZO-1 homology (PDZ) scaffold proteins at the single molecule level reveals an unexpected role of the NR2 subunit divalent arrangement in providing specific anchoring within synapses, highlighting the need to study such dynamic interactions in native conditions.
Biomimetic divalent ligands for the acute disruption of synaptic AMPAR stabilization.
TLDR
Biomimetic competing ligands that are assembled from two Stargazin-derived PSD-95/DLG/ZO-1 (PDZ) domain-binding motifs using 'click' chemistry provide evidence for a model in which the TARP-containing AMPARs are stabilized at the synapse by engaging in multivalent interactions.
In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation.
TLDR
Campylobacter jejuni has a general N-linked glycosylation pathway, which culminates in the transfer of a heptasaccharide from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the asparagine side chain of proteins at the Asn-X-Ser/Thr motif.
From peptide to protein: comparative analysis of the substrate specificity of N-linked glycosylation in C. jejuni.
TLDR
Interestingly, despite recent reports of relaxed selectivity toward the glycan donor, PglB was not found to be capable of utilizing glycosyl donors such as dolichyl-pyrophosphate-chitobiose, which is the minimum substrate for the eukaryotic OT process.
Crystal Structure and Catalytic Mechanism of PglD from Campylobacter jejuni*
TLDR
The co-crystal structures of PglD in the presence of citrate, acetyl coenzyme A, or the UDP-4-amino-sugar were solved, and results from functional assays on alanine mutants suggest His-125 is critical for catalysis, whereas His-15 and His-134 are involved in substrate binding.
In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis.
TLDR
A biochemical approach was taken using recombinant Alg2 and Alg11 from S. cerevisiae and defined dolichylpyrophosphate-linked substrates and the elucidation of the dual function of each of these enzymes completed the identification of the entire ensemble of glycosyltransferases that comprise the dlichol pathway.
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