Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Lizak, C.; Gerber, S.; Numao, S.; Aebi, M.; Locher, K.
    X-ray structure of a bacterial oligosaccharyltransferase (2011), Nature, 474, 350-356.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.99.19 gene pglB, expression of His10-tagged wild-type and mutant enzymes in Escherichia coli strain SCM6 Campylobacter lari

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.99.19 PglB crystal structure analysis Campylobacter jejuni
2.4.99.19 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

EC Number Protein Variants Comment Organism
2.4.99.19 D154A the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme Campylobacter lari
2.4.99.19 D56A the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme Campylobacter lari
2.4.99.19 D56A/E319A the double mutant is inactive Campylobacter lari
2.4.99.19 E319A the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme Campylobacter lari

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.99.19 membrane transmembrane protein Campylobacter jejuni 16020
-
2.4.99.19 membrane transmembrane protein Campylobacter lari 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.99.19 Mg2+ the physiological cation is Mn2+, but PglB is also active with Mg2+ Campylobacter jejuni
2.4.99.19 Mg2+ the physiological cation is Mn2+, but PglB is also active with Mg2+ Campylobacter lari
2.4.99.19 Mn2+ the physiological cation is Mn2+, but PglB is also active with Mg2+ Campylobacter jejuni
2.4.99.19 Mn2+ the physiological cation is Mn2+, but PglB is also active with Mg2+ Campylobacter lari

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.4.99.19 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 ?
2.4.99.19 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

EC Number Organism UniProt Comment Textmining
2.4.99.19 Campylobacter jejuni
-
 gene pglB
-
2.4.99.19 Campylobacter lari B9KDD4 gene pglB
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.4.99.19 glycoprotein functional PglB is partially autoglycosylated at N535 and N556 Campylobacter lari

Purification (Commentary)

EC Number Purification (Comment) Organism
2.4.99.19 recombinant His10-tagged wild-type and mutant enzymes from Escherichia coli strain SCM6 Campylobacter lari

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.99.19 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 ?
2.4.99.19 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 ?
2.4.99.19 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 ?
2.4.99.19 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

EC Number Subunits Comment Organism
2.4.99.19 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

EC Number Synonyms Comment Organism
2.4.99.19 bacterial oligosaccharyltransferase
-
 Campylobacter jejuni
2.4.99.19 bacterial oligosaccharyltransferase
-
 Campylobacter lari
2.4.99.19 bacterial OST
-
 Campylobacter jejuni
2.4.99.19 bacterial OST
-
 Campylobacter lari
2.4.99.19 PglB
-
 Campylobacter jejuni
2.4.99.19 PglB
-
 Campylobacter lari

General Information

EC Number General Information Comment Organism
2.4.99.19 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
2.4.99.19 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