Cloned (Comment) | Organism |
---|---|
gene pglB, expression of His10-tagged wild-type and mutant enzymes in Escherichia coli strain SCM6 | Campylobacter lari |
Crystallization (Comment) | Organism |
---|---|
PglB crystal structure analysis | Campylobacter jejuni |
PglB in complex with acceptor hexapeptide DQNATF, X-ray diffraction structure determination and analysis at 3.4 A resolution, molecular replacement using the periplasmic domain of Campylobacter jejuni PglB, PDB ID 3AAG, as model | Campylobacter lari |
Protein Variants | Comment | Organism |
---|---|---|
D154A | the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme | Campylobacter lari |
D56A | the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme | Campylobacter lari |
D56A/E319A | the double mutant is inactive | Campylobacter lari |
E319A | the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme | Campylobacter lari |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | transmembrane protein | Campylobacter jejuni | 16020 | - |
membrane | transmembrane protein | Campylobacter lari | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the physiological cation is Mn2+, but PglB is also active with Mg2+ | Campylobacter jejuni | |
Mg2+ | the physiological cation is Mn2+, but PglB is also active with Mg2+ | Campylobacter lari | |
Mn2+ | the physiological cation is Mn2+, but PglB is also active with Mg2+ | Campylobacter jejuni | |
Mn2+ | the physiological cation is Mn2+, but PglB is also active with Mg2+ | Campylobacter lari |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | Campylobacter jejuni | - |
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | Campylobacter lari | - |
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Campylobacter jejuni | - |
gene pglB | - |
Campylobacter lari | B9KDD4 | gene pglB | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
glycoprotein | functional PglB is partially autoglycosylated at N535 and N556 | Campylobacter lari |
Purification (Comment) | Organism |
---|---|
recombinant His10-tagged wild-type and mutant enzymes from Escherichia coli strain SCM6 | Campylobacter lari |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | - |
Campylobacter jejuni | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | - |
Campylobacter lari | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing a DQNAT acceptor sequon | Campylobacter lari | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? | |
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine | i.e. substrate peptide LLO, modelling of active site binding, overview, and glycosylation acceptor protein 3D5, a single-chain Fv fragment containing aDQNATacceptor sequon | Campylobacter jejuni | tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide | a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine | ? |
Subunits | Comment | Organism |
---|---|---|
More | PglB possesses a transmembrane domain comprising residues 1-432 and a periplasmic domain comprising residues 433-712, two domains have extensive non-covalent interactions, provided mainly by the first external loop of the transmembrane domain that forms two helices parallel to the membrane plane. The central, catalytic enzyme of OST is the STT3 subunit, structure, overview | Campylobacter lari |
Synonyms | Comment | Organism |
---|---|---|
bacterial oligosaccharyltransferase | - |
Campylobacter jejuni |
bacterial oligosaccharyltransferase | - |
Campylobacter lari |
bacterial OST | - |
Campylobacter jejuni |
bacterial OST | - |
Campylobacter lari |
PglB | - |
Campylobacter jejuni |
PglB | - |
Campylobacter lari |
General Information | Comment | Organism |
---|---|---|
additional information | the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship | Campylobacter jejuni |
additional information | the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship | Campylobacter lari |