ArticleBiochemistry2015
Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic Core.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Quorum sensing regulates a polysaccharide biosynthesis gene to control cell aggregation inISME communications · 2026Article
- Detergent exchange from lipid nanoparticles into detergent micelles unlocks a tool for biochemical and kinetic characterization of membrane proteins.bioRxiv : the preprint server for 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
- 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
- The surprising structural and mechanistic dichotomy of membrane-associated phosphoglycosyl transferases.Biochemical Society transactions · 2021Review
- Prediction of Selected Biosynthetic Pathways for the Lipopolysaccharide Components inPathogens (Basel, Switzerland) · 2021Article
- 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
- A Strategic Approach for Fluorescence Imaging of Membrane Proteins in a Native-like Environment.Cell chemical biology · 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
- Membrane association of monotopic phosphoglycosyl transferase underpins function.Nature chemical biology · 2018Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Phosphoglycosyltransferases (PGTs) catalyze the transfer of a C1'-phosphosugar from a soluble sugar nucleotide diphosphate to a polyprenol phosphate. These enzymes act at the membrane interface, forming the first membrane-associated intermediates in the biosynthesis of cell-surface glycans and glycoconjugates, including glycoproteins, glycolipids, and the peptidoglycan in bacteria. PGTs vary greatly in both their membrane topologies and their substrate preferences. PGTs, such as MraY and WecA, are polytopic, while other families of uniquely prokaryotic enzymes have only a single predicted transmembrane helix. PglC, a PGT involved in the biosynthesis of N-linked glycoproteins in the enteropathogen Campylobacter jejuni, is representative of one of the structurally most simple members of the diverse family of small bacterial PGT enzymes. Herein, we apply bioinformatics and covariance-weighted distance constraints in geometry- and homology-based model building, together with mutational analysis, to investigate monotopic PGTs. The pool of 15000 sequences that are analyzed include the PglC-like enzymes, as well as sequences from two other related PGTs that contain a "PglC-like" domain embedded in their larger structures (namely, the bifunctional PglB family, typified by PglB from Neisseria gonorrheae, and WbaP-like enzymes, typified by WbaP from Salmonella enterica). Including these two subfamilies of PGTs in the analysis highlights key residues conserved across all three families of small bacterial PGTs. Mutagenesis analysis of these conserved residues provides further information about the essentiality of many of these residues in catalysis. Construction of a structural model of the cytosolic globular domain utilizing three-dimensional distance constraints, provided by conservation covariance analysis, provides additional insight into the catalytic core of these families of small bacterial PGT enzymes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.