ReviewBiochemical Society transactions2021
The surprising structural and mechanistic dichotomy of membrane-associated phosphoglycosyl transferases.
Review in Biochemical Society transactions, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Article
- Correlating membrane-protein dynamics with function: Integrating bioinformatics, molecular dynamics, and single-molecule FRET.Protein science : a publication of the Protein Society · 2025Article
- O-antigen polysaccharides inMicrobiology and molecular biology reviews : MMBR · 2025Review
- Mechanisms governing bacterial capsular polysaccharide attachment and chain length.Annals of the New York Academy of Sciences · 2025Review
- Structure of WzxE the lipid III flippase for Enterobacterial Common Antigen polysaccharide.Open biology · 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
- Article
- Uridine Bisphosphonates Differentiate Phosphoglycosyl Transferase Superfamilies.Journal of the American Chemical Society · 2024Article
- Mapping the architecture of the initiating phosphoglycosyl transferase frombioRxiv : the preprint server for biology · 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
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Authors and funding
4 authors.
Funding
Abstract
Phosphoglycosyl transferases (PGTs) play a pivotal role at the inception of complex glycoconjugate biosynthesis pathways across all domains of life. PGTs promote the first membrane-committed step in the en bloc biosynthetic strategy by catalyzing the transfer of a phospho-sugar from a nucleoside diphospho-sugar to a membrane-resident polyprenol phosphate. Studies on the PGTs have been hampered because they are integral membrane proteins, and often prove to be recalcitrant to expression, purification and analysis. However, in recent years exciting new information has been derived on the structures and the mechanisms of PGTs, revealing the existence of two unique superfamilies of PGT enzymes that enact catalysis at the membrane interface. Genome neighborhood analysis shows that these superfamilies, the polytopic PGT (polyPGT) and monotopic PGT (monoPGT), may initiate different pathways within the same organism. Moreover, the same fundamental two-substrate reaction is enacted through two different chemical mechanisms with distinct modes of catalysis. This review highlights the structural and mechanistic divergence between the PGT enzyme superfamilies and how this is reflected in differences in regulation in their varied glycoconjugate biosynthesis pathways.
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