Crystal Structure of a Histidine Kinase Sensor Domain with Similarity to Periplasmic Binding Proteins
Histidine kinase receptors are elements of the two-component signal transduction systems commonly found in bacteria and lower eukaryotes, where they are crucial for environmental adaption through the coupling of extracellular changes to intracellular responses. The typical two-component system consists of a membrane-spanning histidine kinase sensor and a cytoplasmic response regulator. In the calssic system, extracellular signals such as small molecule ligands and ions are detected by the periplasmic sensor domain of the histidine kinase receptor, which modulates the catalytic activity of the cytoplasmic histidine kinase domain and promotes ATP-dependent autophosphorylation of a conserved histidine residue. G. sulfurreducens genomic DNA was used.
- Research Organization:
- Brookhaven National Laboratory (BNL) National Synchrotron Light Source
- Sponsoring Organization:
- Doe - Office Of Science
- DOE Contract Number:
- AC02-98CH10886
- OSTI ID:
- 980097
- Report Number(s):
- BNL--93015-2010-JA
- Journal Information:
- Proteins: Structure, Functions, and Bioinformatics, Journal Name: Proteins: Structure, Functions, and Bioinformatics Journal Issue: 1 Vol. 77
- Country of Publication:
- United States
- Language:
- English
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