Expression and characterization of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies

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Title
Expression and characterization of the integral membrane domain of bacterial histidine kinase SCO3062 for structural studies
Author(s)
K J Yeo; Su Nam Gwak; H J Kim; C Cheong; Myung Hee Kim; Y H Jeon
Bibliographic Citation
Biochemical and Biophysical Research Communications, vol. 376, no. 2, pp. 409-413
Publication Year
2008
Abstract
Bacterial histidine kinases play an important role in the response to external stimuli. Structural studies of the histidine kinase transmembrane domain are challenging due to difficulties in protein expression and sample preparation. After carrying out expression screening of a series of histidine kinases, we investigated sample preparation methods for obtaining high quality samples of the periplasmic and transmembrane domain (PTD) of the bacterial histidine kinase SCO3062. Various sample conditions were tested for their ability to give homogeneous NMR spectra of the SCO3062 PTD with well-resolved resonances. Circular dichroism and 3D 15N-edited NOESY spectrum results demonstrate that the SCO3062 PTD is predominantly α-helical. This method should be applicable to the NMR analysis of other transmembrane proteins.
Keyword
Hemoglobin fusionHistidine kinaseIntegral membrane proteinNMRNuclear magnetic resonanceSCO3062
ISSN
0006-291X
Publisher
Elsevier
DOI
http://dx.doi.org/10.1016/j.bbrc.2008.09.002
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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