ArticleScientific reports2015
Topological analysis of the Escherichia coli WcaJ protein reveals a new conserved configuration for the polyisoprenyl-phosphate hexose-1-phosphate transferase family.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 41 citations in OpenAlex.
- Article
- 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
- Article
- 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
- Characterization of an atypical Actinobacillus pleuropneumoniae serovar 2 isolate with a rough-type lipopolysaccharide.The Journal of veterinary medical science · 2023Article
- 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
- Characterization of the Exopolysaccharide Biosynthesis Pathway in Myxococcus xanthus.Journal of bacteriology · 2020Article
- A Strategic Approach for Fluorescence Imaging of Membrane Proteins in a Native-like Environment.Cell chemical biology · 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
- Identification of the Functional Roles of Six Key Proteins in the Biosynthesis of Enterobacteriaceae Colanic Acid.Biochemistry · 2019Article
- Article
- Membrane association of monotopic phosphoglycosyl transferase underpins function.Nature chemical biology · 2018Article
- Bacterial phosphoglycosyl transferases: initiators of glycan biosynthesis at the membrane interface.Glycobiology · 2017Review
- Functional Interaction between the N and C Termini of NhaD Antiporters from Halomonas sp. Strain Y2.Journal of bacteriology · 2017Article
- Colanic Acid Intermediates Prevent De Novo Shape Recovery of Escherichia coli Spheroplasts, Calling into Question Biological Roles Previously Attributed to Colanic Acid.Journal of bacteriology · 2016Article
- Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic Core.Biochemistry · 2015Article
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4 authors at 2 institutions in 2 countries.
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Abstract
WcaJ is an Escherichia coli membrane enzyme catalysing the biosynthesis of undecaprenyl-diphosphate-glucose, the first step in the assembly of colanic acid exopolysaccharide. WcaJ belongs to a large family of polyisoprenyl-phosphate hexose-1-phosphate transferases (PHPTs) sharing a similar predicted topology consisting of an N-terminal domain containing four transmembrane helices (TMHs), a large central periplasmic loop, and a C-terminal domain containing the fifth TMH (TMH-V) and a cytosolic tail. However, the topology of PHPTs has not been experimentally validated. Here, we investigated the topology of WcaJ using a combination of LacZ/PhoA reporter fusions and sulfhydryl labelling by PEGylation of novel cysteine residues introduced into a cysteine-less WcaJ. The results showed that the large central loop and the C-terminal tail both reside in the cytoplasm and are separated by TMH-V, which does not fully span the membrane, likely forming a "hairpin" structure. Modelling of TMH-V revealed that a highly conserved proline might contribute to a helix-break-helix structure in all PHPT members. Bioinformatic analyses show that all of these features are conserved in PHPT homologues from Gram-negative and Gram-positive bacteria. Our data demonstrate a novel topological configuration for PHPTs, which is proposed as a signature for all members of this enzyme family.
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