ArticleNature communications2018
Structural basis for arginine glycosylation of host substrates by bacterial effector proteins.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
44 citing papers in PubMed, 1 synthesis or guideline pooled it, 61 citations in OpenAlex.
- Recent progress in molecular mechanisms of Salmonella effectors involved in gut epithelium invasion.Molecular biology reports · 2025Pooled it
- Transition-state analysis of the arginine-specific human ADP-ribosyltransferase 1.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of Bacterial ArginineACS catalysis · 2026Article
- Structural insights for enhanced ROS detoxification of eKatE, a recently identified catalase in atypical E. coli.The FEBS journal · 2026Article
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- Interactions between Inhibitors and 5-Lipoxygenase: Insights from Gaussian Accelerated Molecular Dynamics and Markov State Models.International journal of molecular sciences · 2024Article
- Activation of Polycystin-1 Signaling by Binding of Stalk-derived Peptide Agonists.bioRxiv : the preprint server for biology · 2024Article
- Arginine Kinase Activates Arginine for Phosphorylation by Pyramidalization and Polarization.ACS catalysis · 2024Article
- Deciphering the molecular choreography of Janus kinase 2 inhibition via Gaussian accelerated molecular dynamics simulations: a dynamic odyssey.Journal of computer-aided molecular design · 2024Article
- Mechanistic Insights into Peptide Binding and Deactivation of an Adhesion G Protein-Coupled Receptor.Molecules (Basel, Switzerland) · 2023Article
- Salmonella T3SS effector SseK1 arginine-glycosylates the two-component response regulator OmpR to alter bile salt resistance.Scientific reports · 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
- Speaking the host language: howMicrobiology (Reading, England) · 2023Review
- Article
- Catalytic DxD motif caged in Asx-turn and Met-aromatic interaction attenuates the pathogenic glycosylation of SseK2/NleB2 effectors.Scientific reports · 2022Article
- Arginine glycosylation regulates UDP-GlcNAc biosynthesis in Salmonella enterica.Scientific reports · 2022Article
- Repurposing Avasimibe to Inhibit Bacterial Glycosyltransferases.Pathogens (Basel, Switzerland) · 2022Article
- Glycosylating Effectors ofBiomolecules · 2022Review
- Mechanism of RNA recognition by a Musashi RNA-binding protein.Current research in structural biology · 2022Review
Corrections and comments
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Authors and funding
17 authors at 4 institutions in 4 countries.
Funding
Abstract
The bacterial effector proteins SseK and NleB glycosylate host proteins on arginine residues, leading to reduced NF-κB-dependent responses to infection. Salmonella SseK1 and SseK2 are E. coli NleB1 orthologs that behave as NleB1-like GTs, although they differ in protein substrate specificity. Here we report that these enzymes are retaining glycosyltransferases composed of a helix-loop-helix (HLH) domain, a lid domain, and a catalytic domain. A conserved HEN motif (His-Glu-Asn) in the active site is important for enzyme catalysis and bacterial virulence. We observe differences between SseK1 and SseK2 in interactions with substrates and identify substrate residues that are critical for enzyme recognition. Long Molecular Dynamics simulations suggest that the HLH domain determines substrate specificity and the lid-domain regulates the opening of the active site. Overall, our data suggest a front-face S
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Registered trials
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.