ArticleProceedings of the National Academy of Sciences of the United States of America2010
Identical phosphatase mechanisms achieved through distinct modes of binding phosphoprotein substrate.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
What it found
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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
36 citing papers in PubMed, 49 citations in OpenAlex.
- Distinct PlzC mechanisms integrate chemotaxis and c-di-GMP signaling to regulateProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Altering chemotaxis as a strategy to enhance the foraging range of motility-restricted bacteria.Communications biology · 2026Article
- Phosphorylation chemistry of the Bordetella PlrSR TCS and its contribution to bacterial persistence in the lower respiratory tract.Molecular microbiology · 2023Article
- The Interaction Network and Signaling Specificity of Two-Component System inInternational journal of molecular sciences · 2020Review
- Modulation of Response Regulator CheY Reaction Kinetics by Two Variable Residues That Affect Conformation.Journal of bacteriology · 2020Article
- We're in this Together: Sensation of the Host Cell Environment by Endosymbiotic Bacteria.Results and problems in cell differentiation · 2020Article
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- Borrelia burgdorferi CheY2 Is Dispensable for Chemotaxis or Motility but Crucial for the Infectious Life Cycle of the Spirochete.Infection and immunity · 2017Article
- Regulation of signaling directionality revealed by 3D snapshots of a kinase:regulator complex in action.eLife · 2016Article
- The Borrelia burgdorferi CheY3 response regulator is essential for chemotaxis and completion of its natural infection cycle.Cellular microbiology · 2016Article
- Catalytic scaffolds for phosphoryl group transfer.Current opinion in structural biology · 2016Review
- A Variable Active Site Residue Influences the Kinetics of Response Regulator Phosphorylation and Dephosphorylation.Biochemistry · 2016Article
- Molecular Mechanisms of Two-Component Signal Transduction.Journal of molecular biology · 2016Review
- Borrelia burgdorferi CheD Promotes Various Functions in Chemotaxis and the Pathogenic Life Cycle of the Spirochete.Infection and immunity · 2016Article
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- Imidazole as a Small Molecule Analogue in Two-Component Signal Transduction.Biochemistry · 2015Article
- Probing Mechanistic Similarities between Response Regulator Signaling Proteins and Haloacid Dehalogenase Phosphatases.Biochemistry · 2015Article
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- The cyclic-di-GMP signaling pathway in the Lyme disease spirochete, Borrelia burgdorferi.Frontiers in cellular and infection microbiology · 2014Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Two-component signal transduction systems are widespread in prokaryotes and control numerous cellular processes. Extensive investigation of sensor kinase and response regulator proteins from many two-component systems has established conserved sequence, structural, and mechanistic features within each family. In contrast, the phosphatases which catalyze hydrolysis of the response regulator phosphoryl group to terminate signal transduction are poorly understood. Here we present structural and functional characterization of a representative of the CheC/CheX/FliY phosphatase family. The X-ray crystal structure of Borrelia burgdorferi CheX complexed with its CheY3 substrate and the phosphoryl analogue reveals a binding orientation between a response regulator and an auxiliary protein different from that shared by every previously characterized example. The surface of CheY3 containing the phosphoryl group interacts directly with a long helix of CheX which bears the conserved (E - X(2) - N) motif. Conserved CheX residues Glu96 and Asn99, separated by a single helical turn, insert into the CheY3 active site. Structural and functional data indicate that CheX Asn99 and CheY3 Thr81 orient a water molecule for hydrolytic attack. The catalytic residues of the CheX.CheY3 complex are virtually superimposable on those of the Escherichia coli CheZ phosphatase complexed with CheY, even though the active site helices of CheX and CheZ are oriented nearly perpendicular to one other. Thus, evolution has found two structural solutions to achieve the same catalytic mechanism through different helical spacing and side chain lengths of the conserved acid/amide residues in CheX and CheZ.
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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.