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Information on EC 2.4.99.21 - dolichyl-phosphooligosaccharide-protein glycotransferase
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2.4.99.21 dolichyl-phosphooligosaccharide-protein glycotransferaseIUBMB Comments
The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC 2.4.99.18, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is alpha,omega-saturated and it may have additional unsaturated positions in the chain.
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cell-cycle
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retinoblastoma
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p21cip1
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e-cdk2
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r-roscovitine
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Reaction Schemes
Synonyms
aglb protein, archaeal oligosaccharyl transferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AglB
AglB protein
aglB1
AlgB
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine = an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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PATHWAY SOURCE
PATHWAYS
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,
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-phosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase
The enzyme, characterized from the archaea Methanococcus voltae and Haloferax volcanii, transfers a glycan component from dolichyl phosphooligosaccharide to external proteins. It is different from EC 2.4.99.18, dolichyl-diphosphooligosaccharide-protein glycotransferase, which uses dolichyl diphosphate as carrier compound in bacteria and eukaryotes. The enzyme participates in the N-glycosylation of proteins in some archaea. It requires Mn2+. Dolichol used by archaea is different from that used by eukaryotes. It is much shorter (C55-C60), it is alpha,omega-saturated and it may have additional unsaturated positions in the chain.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + Ac-YKYQESSYK-(4-nitro)F-NH2
dolichol + ?
the peptide is based on the sequence of the natively glycosylated flagellum protein FlaB2. The enzyme shows no activity with the peptide Ac-YKYQESSYK-(4-nitro)F-NH2, lacking the key asparagine residue. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
-
-
?
dolichyl 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl phosphate + [flagellum protein FlaB2]-L-asparagine
dolichol + 3-O-(2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyl)-N-acetyl-alpha-D-glucosaminyl-[flagellum protein FlaB2]-L-asparagine
the enzyme is incubated with the acceptor peptide Ac-YKYQESSYK-(4-nitro)F-NH2, which is based the natively glycosylated flagellum protein FlaB2 sequence. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
-
-
?
dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101
dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide, the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
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-
?
dolichyl phosphosulfoheptasaccharide + [protein]-L-asparagine
dolichyl phosphate + a glycoprotein with the sulfoheptasaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
-
-
-
?
lipid-linked oligosaccharide + [peptide]-L-asparagine
lipid + a glycopeptide with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the glycan structure is estimated to be a branched heptasaccharide
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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
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the oligosaccharide chain that Archaeoglobus fulgidus AglB-L transfers to the Asn residues in proteins has the structure alpha-D-Glcp-(1-6)-alpha-[(1-3)-alpha-D-GlcP]-D-Manp-(1-3)-alpha-D-Galp-(1-2)-alpha-D-Manp-(1-3)-[(1-4)-beta-D-Glcp]-beta-D-Galp-(1-4)-beta-D-Glcp-Asn. The monosaccharide residue that is directly linked to the Asn residue is hexose
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?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively
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-
?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
-
-
?
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
the Pyrococcus furiosus and Archaeoglobus fulgidus AglBs preferentially glycosylate sequons with Val and Glu at the X position, respectively
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-
?
additional information
?
-
tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex
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additional information
?
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tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex. The tethered peptide serves as an efficient substrate that receives the oligosaccharide chain from the lipid-linked oligosaccharide. The oligosaccharyl transfer is a single-turnover reaction, because it proceeds within the covalently cross-linked complex
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additional information
?
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the enzyme (AglB) has the ability to attach incomplete glycans as seen by the disaccharides present on flagellins and S-layer proteins in Methanococcus voltae aglA mutant cells. AglA is the glycosyl transferase involved in the attachment of the terminal sugar to the glycan
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an archaeal dolichyl phosphooligosaccharide + [protein]-L-asparagine
an archaeal dolichyl phosphate + a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
-
-
?
dolichyl phosphooligosaccharide + [flagellum protein FlaB2]-L-asparagine101
dolichol + flagellum protein FlaB2 with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. The activity is dependent on the canonical AsnXaaSer/Thr sequon. Although the full length N-glycan generated by Methanococcus voltae (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine) is a trisaccharide, the disaccharide-linked substrate is sufficient for oligosaccharyl transferase activity
-
-
?
dolichyl phosphosulfoheptasaccharide + [protein]-L-asparagine
dolichyl phosphate + a glycoprotein with the sulfoheptasaccharide chain attached by N-beta-D-glycosyl linkage to a protein L-asparagine
-
-
-
-
?
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the recombinant enzyme is purified from membrane fraction from Escherichia coli
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
wild-type cells are motile, mutant cells (with an insertional inactivation of the aglB gene) are non-motile. The mutant cells have detectable shifts in flagellin molecular weight. Thea are non-flaggelated, since only N-terminally processed flagellins can be assembled into flagella filaments
malfunction
an aglB deletion mutant is not flagellated. The pili of the DELTAaglB strain form thick bundles containing multiple filaments, and the lack of AglB-dependent glycosylation in this strain promotes microcolony formation
malfunction
a strain deleted of aglB, encoding the archaeal oligosaccharyltransferase, is generated. In this DELTAaglB strain, archaella are not detected and only low levels of archaellins are released into the medium, in contrast to the parent strain. Mass spectrometry analysis of the archaellins in DELTAaglB cultures did not detect N-glycosylation. DELTAaglB cells showed a slight growth defect and are impaired for motility. N-glycosylation is important for archaellum assembly and cell motility in Halobacterium salinarum, as well as for archaellin gene transcription and translation
malfunction
-
AglBs from Methanococcus voltae and Methanothermococcus thermolithotrophicus functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain, both returning the apparent molecular weight of archaellin FlaB2 to wild type size and restoring archaellation. Attempts to use AglB from Methanocaldococcus jannaschii, Haloferax volcanii or Sulfolobus acidocaldarius to functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain are unsuccessful
malfunction
-
AglBs from Methanococcus voltae and Methanothermococcus thermolithotrophicus functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain, both returning the apparent molecular weight of archaellin FlaB2 to wild type size and restoring archaellation. Attempts to use AglB from Methanocaldococcus jannaschii, Haloferax volcanii or Sulfolobus acidocaldarius to functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain are unsuccessful
malfunction
AglBs from Methanococcus voltae and Methanothermococcus thermolithotrophicus functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain, both returning the apparent molecular weight of archaellin FlaB2 to wild type size and restoring archaellation. Attempts to use AglB from Methanocaldococcus jannaschii, Haloferax volcanii or Sulfolobus acidocaldarius to functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain are unsuccessful
malfunction
-
AglBs from Methanococcus voltae and Methanothermococcus thermolithotrophicus functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain, both returning the apparent molecular weight of archaellin FlaB2 to wild type size and restoring archaellation. Attempts to use AglB from Methanocaldococcus jannaschii, Haloferax volcanii or Sulfolobus acidocaldarius to functionally replace the oligosaccharyltransferase activity missing in the Methanococcus maripaludis DELTAaglB strain are unsuccessful
-
malfunction
-
a strain deleted of aglB, encoding the archaeal oligosaccharyltransferase, is generated. In this DELTAaglB strain, archaella are not detected and only low levels of archaellins are released into the medium, in contrast to the parent strain. Mass spectrometry analysis of the archaellins in DELTAaglB cultures did not detect N-glycosylation. DELTAaglB cells showed a slight growth defect and are impaired for motility. N-glycosylation is important for archaellum assembly and cell motility in Halobacterium salinarum, as well as for archaellin gene transcription and translation
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metabolism
the enzyme is involved in the transfer of the complete glycan to the flagellin and S-layer proteins
metabolism
the enzyme participates in the N-linked glycosylation in Methanococcus voltae. It catalyzes transfer of oligosaccharides from the dolichyl phosphate donor to asparagine in the acceptor proteins. Methanococcus voltae generates N-linked glycoproteins with a unique trisaccharide (L-threonyl 2-(acetylamino)-2-deoxy-beta-D-mannuronamido-(1->4)-2,3-bis(acetylamino)-2,3-bis(acetylamino)-2,3-dideoxy-beta-D-glucuronosyl-(1->3)-2-(acetylamino)-2-deoxy-beta-D-glucosyl-[protein]-L-asparagine)
physiological function
cells lacking glycotransferase AglB are unable to N-glycosylate the S-layer glycoprotein. The absence of AglB results in enhanced release of the S-layer glycoprotein. Haloferax volcanii AglB mutant cells grow significantly less well at elevated salt levels than do cells of the background strain
physiological function
-
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB
physiological function
-
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB
physiological function
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB
physiological function
isoform AglB is essential for the viability of Sulfolobus acidocaldarius
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
physiological function
-
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
-
physiological function
-
isoform AglB is essential for the viability of Sulfolobus acidocaldarius
-
physiological function
-
enzyme can readily replace its counterpart from Haloferax volcanii when introduced into Haloferax volcanii cells deleted of glycotransferase aglB
-
physiological function
-
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
-
physiological function
-
cells lacking glycotransferase AglB are unable to N-glycosylate the S-layer glycoprotein. The absence of AglB results in enhanced release of the S-layer glycoprotein. Haloferax volcanii AglB mutant cells grow significantly less well at elevated salt levels than do cells of the background strain
-
Show AA Sequence and Transmembrane Helices (3690 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
additional information
-
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
additional information
-
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
-
additional information
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
additional information
-
the prokaryotic oligosaccharyltransferase enzyme consists of a single polypeptide chain
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein consists of the transmembrane domain, about 400-500 residues, 13 transmembrane helices and long external loops EL1 and EL5 and the CC structural unit in the C-terminal globular domain. The key amino acid residue is the conserved Glu residue in the TIXE/SVXE motif in the EL5 loop
sitting drop vapor diffusion method of G617C mutant protein, the crystal structure of the cross-linked AfAglB-peptide complex is determined to 3.5 A resolution
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, column chromatography, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli with N-terminal T7 and C-terminal His6 tags
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cohen-Rosenzweig, C.; Guan, Z.; Shaanan, B.; Eichler, J.
Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans
Appl. Environ. Microbiol.
80
486-496
2014
Haloarcula marismortui, Haloferax mediterranei, Halobacterium salinarum (B0R4T2), Halobacterium salinarum DSM 671 (B0R4T2)
brenda
Chaban, B.; Voisin, S.; Kelly, J.; Logan, S.M.; Jarrell, K.F.
Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N-linked glycans: insight into N-linked glycosylation pathways in Archaea
Mol. Microbiol.
61
259-268
2006
Methanococcus voltae (Q2EMT4)
brenda
Larkin, A.; Chang, M.M.; Whitworth, G.E.; Imperiali, B.
Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis
Nat. Chem. Biol.
9
367-373
2013
Methanococcus voltae (Q2EMT4), Methanococcus voltae
brenda
Fujinami, D.; Nyirenda, J.; Matsumoto, S.; Kohda, D.
Structural elucidation of an asparagine-linked oligosaccharide from the hyperthermophilic archaeon, Archaeoglobus fulgidus
Carbohydr. Res.
413
55-62
2015
Archaeoglobus fulgidus (O29867)
brenda
Abu-Qarn, M.; Yurist-Doutsch, S.; Giordano, A.; Trauner, A.; Morris, H.R.; Hitchen, P.; Medalia, O.; Dell, A.; Eichler, J.
Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer
J. Mol. Biol.
374
1224-1236
2007
Haloferax volcanii (D4GYH4), Haloferax volcanii DSM 3757 (D4GYH4)
brenda
Meyer, B.H.; Albers, S.V.
AglB, catalyzing the oligosaccharyl transferase step of the archaeal N-glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius
MicrobiologyOpen
3
531-543
2014
Sulfolobus acidocaldarius (Q4J9B4), Sulfolobus acidocaldarius DSM 639 (Q4J9B4)
brenda
Matsumoto, S.; Shimada, A.; Nyirenda, J.; Igura, M.; Kawano, Y.; Kohda, D.
Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation
Proc. Natl. Acad. Sci. USA
110
17868-17873
2013
Archaeoglobus fulgidus (O29867)
brenda
Esquivel, R.N.; Schulze, S.; Xu, R.; Hippler, M.; Pohlschroder, M.
Identification of Haloferax volcanii pilin N-glycans with diverse roles in pilus biosynthesis, adhesion, and microcolony formation
J. Biol. Chem.
291
10602-10614
2016
Haloferax volcanii (D4GYH4)
brenda
Taguchi, Y.; Fujinami, D.; Kohda, D.
Comparative analysis of archaeal lipid-linked oligosaccharides that serve as oligosaccharide donors for Asn glycosylation
J. Biol. Chem.
291
11042-11054
2016
Archaeoglobus fulgidus
brenda
Kohda, D.
Structural basis of protein Asn-glycosylation by oligosaccharyltransferases
Adv. Exp. Med. Biol.
1104
171-199
2018
Archaeoglobus fulgidus, Pyrococcus furiosus
brenda
Matsumoto, S.; Taguchi, Y.; Shimada, A.; Igura, M.; Kohda, D.
Tethering an N-glycosylation sequon-containing peptide creates a catalytically competent oligosaccharyltransferase complex
Biochemistry
56
602-611
2017
Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus ATCC 49558 (O29867)
brenda
Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
Biomolecules
10
624
2020
Pyrococcus horikoshii (O74088), Pyrococcus horikoshii ATCC 700860 (O74088)
brenda
Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
Biomolecules
10
32316603
2020
Archaeoglobus fulgidus (O29867), Archaeoglobus fulgidus, Archaeoglobus fulgidus ATCC 49558 (O29867)
brenda
Zaretsky, M.; Darnell, C.; Schmid, A.; Eichler, J.
N-Glycosylation is important for Halobacterium salinarum archaellin expression, archaellum assembly and cell motility
Front. Microbiol.
10
1367
2019
Halobacterium salinarum (Q9HQP2), Halobacterium salinarum ATCC 700922 (Q9HQP2)
brenda
Ding, Y.; Vrionis, H.; Schneider, J.; Berezuk, A.; Khursigara, C.; Jarrell, K.
Complementation of an aglB mutant of Methanococcus maripaludis with heterologous oligosaccharyltransferases
PLoS ONE
11
e0167611
2016
Methanococcus maripaludis, Methanothermococcus thermolithotrophicus, Methanococcus voltae (Q2EMT4), Methanothermococcus thermolithotrophicus DSM2095
brenda
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