Allosteric Communication within the Cytoplasmic Region of the Histidine Kinase CpxA, Revealed by Molecular Dynamics Simulations of the Wild-Type and M228V Proteins - Archive ouverte HAL Access content directly
Journal Articles Biophysical Journal Year : 2016

Allosteric Communication within the Cytoplasmic Region of the Histidine Kinase CpxA, Revealed by Molecular Dynamics Simulations of the Wild-Type and M228V Proteins

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1
Nathalie Duclert
Jean-Michel Betton
  • Function : Author
  • PersonId : 920795
Pedro M. Alzari
  • Function : Author
  • PersonId : 858583
Michael Nilges
Therese E. Malliavin

Abstract

The histidine kinases belong to the family of two-component systems, which serves in bacteria to couple environmental stimuli to adaptive responses. Most of the histidine kinases are homodimers, in which the HAMP and DHp domains assemble into an elongated helical region flanked by two CA domains. Recently, X-ray crystallographic structures of the cytoplasmic region of the Escherichia coli histidinekinase CpxA were determined [1] and a phosphotransferase-defective mutant, M228V, located in HAMP, was identified.

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pasteur-01300941 , version 1 (11-04-2016)

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Marlet Martinez, Nathalie Duclert, Jean-Michel Betton, Pedro M. Alzari, Michael Nilges, et al.. Allosteric Communication within the Cytoplasmic Region of the Histidine Kinase CpxA, Revealed by Molecular Dynamics Simulations of the Wild-Type and M228V Proteins. Biophysical Journal, 2016, 108 (2), supplement 1, 184A. ⟨10.1016/j.bpj.2014.11.1016⟩. ⟨pasteur-01300941⟩

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