ArticleProtein science : a publication of the Protein Society2013
Insight into the sporulation phosphorelay: crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed.
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- Amine-recognizing domain in diverse receptors from bacteria and archaea evolved from the universal amino acid sensor.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Is it possible to predict signal molecules that are recognized by bacterial receptors?Environmental microbiology · 2023Article
- Exploring AI-2-mediated interspecies communications within rumen microbial communities.Microbiome · 2022Article
- Cefotaxime Exposure Selects Mutations within the CA-Domain ofMicrobiology spectrum · 2022Article
- Chemotaxis of the Human Pathogen Pseudomonas aeruginosa to the Neurotransmitter Acetylcholine.mBio · 2022Article
- Phylogenetic Analysis with Prediction of Cofactor or Ligand Binding for Pseudomonas aeruginosa PAS and Cache Domains.Microbiology spectrum · 2021Article
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Machine learning uncovers independently regulated modules in the Bacillus subtilis transcriptome.Nature communications · 2020Article
- Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes.Nature communications · 2020Article
- RNA-Seq analysis of differentially expressed genes of Staphylococcus epidermidis isolated from postoperative endophthalmitis and the healthy conjunctiva.Scientific reports · 2020Article
- YycH and YycI Regulate Expression ofMicroorganisms · 2020Article
- Article
- Structural and ligand binding analyses of the periplasmic sensor domain of RsbU in Chlamydia trachomatis support a role in TCA cycle regulation.Molecular microbiology · 2020Article
- Sensor kinase KinB and its pathway-associated key factors sense the signal of nutrition starvation in sporulation of Bacillus subtilis.MicrobiologyOpen · 2018Article
- Article
- Signaling ammonium across membranes through an ammonium sensor histidine kinase.Nature communications · 2018Article
- Methyl-accepting chemotaxis proteins: a core sensing element in prokaryotes and archaea.Cellular and molecular life sciences : CMLS · 2017Review
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Abstract
The Bacillus subtilis KinD signal-transducing histidine kinase is a part of the sporulation phosphorelay known to regulate important developmental decisions such as sporulation and biofilm formation. We have determined crystal structures of the extracytoplasmic sensing domain of KinD, which was copurified and crystallized with a pyruvate ligand. The structure of a ligand-binding site mutant was also determined; it was copurified and crystallized with an acetate ligand. The structure of the KinD extracytoplasmic segment is similar to that of several other sensing domains of signal transduction proteins and is composed of tandem Per-Arnt-Sim (PAS)-like domains. The KinD ligand-binding site is located on the membrane distal PAS-like domain and appears to be highly selective; a single mutation, R131A, abolishes pyruvate binding and the mutant binds acetate instead. Differential scanning fluorimetry, using a variety of monocarboxylic and dicarboxylic acids, identified pyruvate, propionate, and butyrate but not lactate, acetate, or malate as KinD ligands. A recent report found that malate induces biofilm formation in a KinD-dependent manner. It was suggested that malate might induce a metabolic shift and increased secretion of the KinD ligand of unknown identity. The structure and binding assays now suggests that this ligand is pyruvate and/or other small monocarboxylic acids. In summary, this study gives a first insight into the identity of a molecular ligand for one of the five phosphorelay kinases of B. subtilis.
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