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Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG
Zhao, Haiyan Tang, Liang
Zhao, Haiyan
Tang, Liang
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Abstract
YycGF is a highly conserved two-component signal transduction system that is specific to low-G+C Gram-positive bacteria, including many important human pathogens. It has been recognized as a crucial regulatory system for cell-wall metabolism. YycG, the histidine protein kinase of this system, is a multidomain transmembrane protein. The truncated cytoplasmic portion of YycG from Bacillus subtilis encompassing the PAS domain, the dimerization domain and the catalytic domain was expressed, purified and crystallized. X-ray data were collected to 2.8 Å resolution with a completeness of 98.2% and an overall Rmerge of 5.6%. The crystals belonged to space group P61 or P65, with unit-cell parameters a = 135.0, c = 133.0 Å. The selenomethionine-substituted version of the protein was crystallized and X-ray data were collected to 3.6 Å resolution for subsequent MAD phasing.
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This is the publisher's version, also available electronically from "http://scripts.iucr.org".
Date
2009-04-01
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International Union of Crystallography
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Keywords
histidine protein kinases, Two-component systems, Signal transduction, Gram-positive bacteria, cell wall, PAS domains, YycG, YycF, Autophosphorylation
Citation
Zhao, H., & Tang, L. (2009). Crystallographic characterization of the histidine protein kinase from an essential two-component regulatory system YycFG. Acta Crystallografica F Struct Biol Cryst Commun., 64(4), 346-349. http://www.dx.doi.org/10.1107/S174430910900668X