Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB

Cheung, J; Hendrickson, W

doi:10.1074/jbc.M805253200

Title: Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB

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Abstract

Two-component signaling systems allow bacteria to adapt to changing environments. Typically, a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane in histidine kinases are not fully understood. In an effort to further understand such processes, we have solved the crystal structures of the periplasmic sensor domains of Escherichia coli DcuS and of Vibrio cholerae DctB in complex with the respective cognate ligands, malate and succinate. Both proteins are involved in the regulation of the transport and metabolism of C{sub 4-}dicarboxylates, but they are not highly related by sequence similarity. Our work reveals that despite disparate sizes, both structures contain a similar characteristic {alpha}/{beta} PDC (PhoQ-DcuS-CitA) sensor-domain fold and display similar modes of ligand binding, suggesting similar mechanisms of function.

Authors:: Cheung, J; Hendrickson, W

Publication Date:: Tue Jan 01 00:00:00 EST 2008

Research Org.:: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source

Sponsoring Org.:: Doe - Office Of Science

OSTI Identifier:: 980112

Report Number(s):: BNL-93030-2010-JA
Journal ID: ISSN 0021-9258; JBCHA3; TRN: US201015%%1497

DOE Contract Number:: DE-AC02-98CH10886

Resource Type:: Journal Article

Journal Name:: Journal of Biological Chemistry

Additional Journal Information:: Journal Volume: 283; Journal ID: ISSN 0021-9258

Country of Publication:: United States

Language:: English

Subject:: 36 MATERIALS SCIENCE; 59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; BACTERIA; CELL MEMBRANES; COMPLEXES; CRYSTAL STRUCTURE; ESCHERICHIA COLI; GENES; HISTIDINE; LIGANDS; METABOLISM; PHOSPHOTRANSFERASES; PROTEINS; REGULATIONS; RELAYS; SIGNALS; TRANSPORT; national synchrotron light source

Citation Formats


                    Cheung, J, and Hendrickson, W. Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB.  United States: N. p., 2008. 
        Web.  doi:10.1074/jbc.M805253200.

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                    Cheung, J, & Hendrickson, W. Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB.  United States.  https://doi.org/10.1074/jbc.M805253200

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                    Cheung, J, and Hendrickson, W. 2008.  
        "Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB".  United States.  https://doi.org/10.1074/jbc.M805253200.

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@article{osti_980112,

  title        = {Crystal Structures of C4-Dicarboxylate Ligand Complexes with Sensor Domains of Histidine Kinases DcuS and DctB},

  author       = {Cheung, J and Hendrickson, W},

  abstractNote = {Two-component signaling systems allow bacteria to adapt to changing environments. Typically, a chemical or other stimulus is detected by the periplasmic sensor domain of a transmembrane histidine kinase sensor, which in turn relays a signal through a phosphotransfer cascade to the cognate cytoplasmic response regulator. Such systems lead ultimately to changes in gene expression or cell motility. Mechanisms of ligand binding and signal transduction through the cell membrane in histidine kinases are not fully understood. In an effort to further understand such processes, we have solved the crystal structures of the periplasmic sensor domains of Escherichia coli DcuS and of Vibrio cholerae DctB in complex with the respective cognate ligands, malate and succinate. Both proteins are involved in the regulation of the transport and metabolism of C{sub 4-}dicarboxylates, but they are not highly related by sequence similarity. Our work reveals that despite disparate sizes, both structures contain a similar characteristic {alpha}/{beta} PDC (PhoQ-DcuS-CitA) sensor-domain fold and display similar modes of ligand binding, suggesting similar mechanisms of function.},

  doi          = {10.1074/jbc.M805253200},

  url          = {https://www.osti.gov/biblio/980112},
  journal      = {Journal of Biological Chemistry},

  issn         = {0021-9258},

  number       = ,

  volume       = 283,

  place        = {United States},

  year         = {Tue Jan 01 00:00:00 EST 2008},

  month        = {Tue Jan 01 00:00:00 EST 2008}

}

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