ArticleThe Journal of biological chemistry2014
Sensor domain of histidine kinase KinB of Pseudomonas: a helix-swapped dimer.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Mechanism of sensor kinase CitA transmembrane signaling.Nature communications · 2025Article
- Thermal shift assay to identify ligands for bacterial sensor proteins.FEMS microbiology reviews · 2025Review
- Crystal structures of QseE and QseG: elements of a three-component system from Escherichia coli.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Diversity in Sensing and Signaling of Bacterial Sensor Histidine Kinases.Biomolecules · 2021Review
- Sensor Domain of Histidine Kinase VxrA ofJournal of bacteriology · 2021Article
- Functional Annotation of Bacterial Signal Transduction Systems: Progress and Challenges.International journal of molecular sciences · 2018Review
- Signaling ammonium across membranes through an ammonium sensor histidine kinase.Nature communications · 2018Article
- Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling.The EMBO journal · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The overproduction of polysaccharide alginate is responsible for the formation of mucus in the lungs of cystic fibrosis patients. Histidine kinase KinB of the KinB-AlgB two-component system in Pseudomonas aeruginosa acts as a negative regulator of alginate biosynthesis. The modular architecture of KinB is similar to other histidine kinases. However, its periplasmic signal sensor domain is unique and is found only in the Pseudomonas genus. Here, we present the first crystal structures of the KinB sensor domain. The domain is a dimer in solution, and in the crystal it shows an atypical dimer of a helix-swapped four-helix bundle. A positively charged cavity is formed on the dimer interface and involves several strictly conserved residues, including Arg-60. A phosphate anion is bound asymmetrically in one of the structures. In silico docking identified several monophosphorylated sugars, including β-D-fructose 6-phosphate and β-D-mannose 6-phosphate, a precursor and an intermediate of alginate synthesis, respectively, as potential KinB ligands. Ligand binding was confirmed experimentally. Conformational transition from a symmetric to an asymmetric structure and decreasing dimer stability caused by ligand binding may be a part of the signal transduction mechanism of the KinB-AlgB two-component system.
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