ArticleProceedings of the National Academy of Sciences of the United States of America2022
Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Architecture of the Wza-Wzc complex that mediates colanic acid translocation across the cell envelope in Gram-negative bacteria.Nature communications · 2026Article
- Molecular insights into the capsular polysaccharide transporter Wza-Wzc complex.Nature communications · 2026Article
- Tyrosine phosphorylation coupling of one-carbon metabolism and virulence in an endogenous pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Identification of EcpK, a bacterial tyrosine pseudokinase important for exopolysaccharide biosynthesis inJournal of bacteriology · 2025Article
- Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc.Nature communications · 2025Article
- Urine-mediated suppression ofmSphere · 2023Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Bacterial tyrosine kinases (BY-kinases) comprise a family of protein tyrosine kinases that are structurally distinct from their functional counterparts in eukaryotes and are highly conserved across the bacterial kingdom. BY-kinases act in concert with their counteracting phosphatases to regulate a variety of cellular processes, most notably the synthesis and export of polysaccharides involved in biofilm and capsule biogenesis. Biochemical data suggest that BY-kinase function involves the cyclic assembly and disassembly of oligomeric states coupled to the overall phosphorylation levels of a C-terminal tyrosine cluster. This process is driven by the opposing effects of intermolecular autophosphorylation, and dephosphorylation catalyzed by tyrosine phosphatases. In the absence of structural insight into the interactions between a BY-kinase and its phosphatase partner in atomic detail, the precise mechanism of this regulatory process has remained poorly defined. To address this gap in knowledge, we have determined the structure of the transiently assembled complex between the catalytic core of the
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Registered trials
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