ArticleThe Journal of biological chemistry2010
Comparative structural biology of eubacterial and archaeal oligosaccharyltransferases.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 90 citations in OpenAlex.
- N-glycosylation in Archaea - Expanding the process, components and roles of a universal post-translational modification.BBA advances · 2024Article
- The Role of Substrate Mediated Allostery in the Catalytic Competency of the Bacterial Oligosaccharyltransferase PglB.Frontiers in molecular biosciences · 2021Article
- Cell-free systems for accelerating glycoprotein expression and biomanufacturing.Journal of industrial microbiology & biotechnology · 2020Review
- Structural Insight into the Mechanism ofBiomolecules · 2020Review
- Oligosaccharyltransferase PglB of Campylobacter jejuni is a glycoprotein.World journal of microbiology & biotechnology · 2019Article
- A Radioisotope-free Oligosaccharyltransferase Assay Method.Bio-protocol · 2019Article
- Stereochemical Divergence of Polyprenol Phosphate Glycosyltransferases.Trends in biochemical sciences · 2018Review
- Sialic Acid-Like Sugars in Archaea: Legionaminic Acid Biosynthesis in the HalophileFrontiers in microbiology · 2018Article
- Structural basis for catalysis at the membrane-water interface.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- The multiple evolutionary origins of the eukaryotic N-glycosylation pathway.Biology direct · 2016Article
- Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation.The Journal of biological chemistry · 2016Article
- ArnT proteins that catalyze the glycosylation of lipopolysaccharide share common features with bacterial N-oligosaccharyltransferases.Glycobiology · 2016Article
- Complementation of an aglB Mutant of Methanococcus maripaludis with Heterologous Oligosaccharyltransferases.PloS one · 2016Article
- An inside-out origin for the eukaryotic cell.BMC biology · 2014Article
- AglB, catalyzing the oligosaccharyl transferase step of the archaeal N-glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.MicrobiologyOpen · 2014Article
- N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014Review
- Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.Applied and environmental microbiology · 2014Article
- Article
- Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases.BMC structural biology · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligosaccharyltransferase (OST) catalyzes the transfer of an oligosaccharide from a lipid donor to an asparagine residue in nascent polypeptide chains. In the bacterium Campylobacter jejuni, a single-subunit membrane protein, PglB, catalyzes N-glycosylation. We report the 2.8 A resolution crystal structure of the C-terminal globular domain of PglB and its comparison with the previously determined structure from the archaeon Pyrococcus AglB. The two distantly related oligosaccharyltransferases share unexpected structural similarity beyond that expected from the sequence comparison. The common architecture of the putative catalytic sites revealed a new catalytic motif in PglB. Site-directed mutagenesis analyses confirmed the contribution of this motif to the catalytic function. Bacterial PglB and archaeal AglB constitute a protein family of the catalytic subunit of OST along with STT3 from eukaryotes. A structure-aided multiple sequence alignment of the STT3/PglB/AglB protein family revealed three types of OST catalytic centers. This novel classification will provide a useful framework for understanding the enzymatic properties of the OST enzymes from Eukarya, Archaea, and Bacteria.
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