ArticleProceedings of the National Academy of Sciences of the United States of America2017
Analysis of a dual domain phosphoglycosyl transferase reveals a ping-pong mechanism with a covalent enzyme intermediate.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 39 citations in OpenAlex.
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
- Proteome-wide bioinformatic annotation and functional validation of the monotopic phosphoglycosyl transferase superfamily.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Proteome-Wide Bioinformatic Annotation and Functional Validation of the Monotopic Phosphoglycosyl Transferase Superfamily.bioRxiv : the preprint server for biology · 2024Article
- Uridine Bisphosphonates Differentiate Phosphoglycosyl Transferase Superfamilies.Journal of the American Chemical Society · 2024Article
- Functional production and biochemical investigation of an integral membrane enzyme for olefin biosynthesis.Protein science : a publication of the Protein Society · 2024Article
- Characterization of PglJ, a Glycosyltransferase in theBiochemistry · 2024Article
- A generalizable protocol for expression and purification of membrane-bound bacterial phosphoglycosyl transferases in liponanoparticles.Protein expression and purification · 2023Article
- Co-conserved sequence motifs are predictive of substrate specificity in a family of monotopic phosphoglycosyl transferases.Protein science : a publication of the Protein Society · 2023Article
- Defining Early Steps inbioRxiv : the preprint server for biology · 2023Article
- Probing Monotopic Phosphoglycosyl Transferases from Complex Cellular Milieu.ACS chemical biology · 2022Article
- Tracking Colanic Acid Repeat Unit Formation from Stepwise Biosynthesis Inactivation inBiochemistry · 2021Article
- The surprising structural and mechanistic dichotomy of membrane-associated phosphoglycosyl transferases.Biochemical Society transactions · 2021Review
- Glycoconjugate pathway connections revealed by sequence similarity network analysis of the monotopic phosphoglycosyl transferases.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Nucleotide Sugars in Chemistry and Biology.Molecules (Basel, Switzerland) · 2020Review
- Comparative Analysis of High-Throughput Assays of Family-1 Plant Glycosyltransferases.International journal of molecular sciences · 2020Article
- General Utilization of Fluorescent Polyisoprenoids with Sugar Selective Phosphoglycosyltransferases.Biochemistry · 2020Article
- Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces.Current opinion in structural biology · 2019Review
- Investigation of the conserved reentrant membrane helix in the monotopic phosphoglycosyl transferase superfamily supports key molecular interactions with polyprenol phosphate substrates.Archives of biochemistry and biophysics · 2019Article
- Monotopic Membrane Proteins Join the Fold.Trends in biochemical sciences · 2019Review
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phosphoglycosyl transferases (PGTs) are integral membrane proteins with diverse architectures that catalyze the formation of polyprenol diphosphate-linked glycans via phosphosugar transfer from a nucleotide diphosphate-sugar to a polyprenol phosphate. There are two PGT superfamilies that differ significantly in overall structure and topology. The polytopic PGT superfamily, represented by MraY and WecA, has been the subject of many studies because of its roles in peptidoglycan and O-antigen biosynthesis. In contrast, less is known about a second, extensive superfamily of PGTs that reveals a core structure with dual domain architecture featuring a C-terminal soluble globular domain and a predicted N-terminal membrane-associated domain. Representative members of this superfamily are the
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