Cloned (Comment) | Organism |
---|---|
gene pglB, sequence and structure comparison with STT3 subunit of the eukaryotic OTase complex of Saccharomyces cerevisiae | Campylobacter jejuni |
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 | Comment | Organism | Structure |
---|---|---|---|
Mn2+ | activates | Campylobacter jejuni |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
gene pglB | - |
Subunits | Comment | Organism |
---|---|---|
monomer | sequence and structure comparison with STT3 subunit of the eukaryotic OST complex | Campylobacter jejuni |
Synonyms | Comment | Organism |
---|---|---|
oligosaccharyl transferase | - |
Campylobacter jejuni |
OTase | - |
Campylobacter jejuni |
PglB | - |
Campylobacter jejuni |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Campylobacter jejuni |
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 |