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Literature summary for 2.4.99.19 extracted from

  • Jaffee, M.B.; Imperiali, B.
    Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases (2011), Biochemistry, 50, 7557-7567.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.4.99.19

Cloned(Commentary)

Cloned (Comment) Organism
gene pglB, sequence and structure comparison with STT3 subunit of the eukaryotic OTase complex of Saccharomyces cerevisiae Campylobacter jejuni

Protein Variants

Protein Variants Comment Organism
D152E site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level Campylobacter jejuni
D475A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Campylobacter jejuni
D475E site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Campylobacter jejuni
D54A site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity Campylobacter jejuni
E316D site-directed mutagenesis, D152 and E316 can both be mutated to their acidic counterparts (D152E and E316D) and still retain activity, albeit at a notably decreased level Campylobacter jejuni
E316Q site-directed mutagenesis, inactive mutant Campylobacter jejuni
K478A site-directed mutagenesis, the mutant shows decreased activity compared to the wild-type enzyme Campylobacter jejuni
K478A site-directed mutagenesis, the increased Und-PP-Bac-GalNAc substrate concentration has little effect on the mutant activity Campylobacter jejuni
additional information the mutations at these sites affects the ability of PglB to bind the polyprenyldiphosphate glycan substrate, but the mutants maintain the tertiary structure Campylobacter jejuni

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ activates Campylobacter jejuni

Organism

Organism UniProt Comment Textmining
Campylobacter jejuni
-
 gene pglB
-

Subunits

Subunits Comment Organism
monomer sequence and structure comparison with STT3 subunit of the eukaryotic OST complex Campylobacter jejuni

Synonyms

Synonyms Comment Organism
oligosaccharyl transferase
-
 Campylobacter jejuni
OTase
-
 Campylobacter jejuni
PglB
-
 Campylobacter jejuni

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Campylobacter jejuni

General Information

General Information Comment Organism
evolution sequence analysis using 28 homologs from evolutionarily distant organisms, relationship between PglB and other Stt3 proteins, detailed overview Several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function Campylobacter jejuni
metabolism the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins Campylobacter jejuni
additional information several inter-transmembrane loop regions of PglB/Stt3 contain strictly conserved motifs that are essential for PglB function, these loops play a fundamental role in catalysis Campylobacter jejuni
physiological function the central enzyme in N-linked glycosylation is the oligosaccharyl transferase PglB, which catalyzes glycan transfer from a polyprenyldiphosphate-linked carrier to select asparagines within acceptor proteins. Role of the intertransmembrane domain loops in OTase catalysis Campylobacter jejuni