Preliminary crystallographic studies of the regulatory domain of response regulator YycF from an essential two-component signal transduction system

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Issue Date
2009-07-01Author
Zhao, Haiyan
Heroux, Annie
Sequeira, Reuben D.
Tang, Liang
Publisher
International Union of Crystallography
Type
Article
Article Version
Scholarly/refereed, publisher version
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Show full item recordAbstract
YycGF is a crucial signal transduction system for the regulation of cell-wall metabolism in low-G+C Gram-positive bacteria, which include many important human pathogens. The response regulator YycF receives signals from its cognate histidine kinase YycG through a phosphotransfer reaction and elicits responses through regulation of gene expression. The N-terminal regulatory domain of YycF from Bacillus subtilis was overproduced and purified. The protein was crystallized and X-ray data were collected to 1.95 Å resolution with a completeness of 97.7% and an overall Rmerge of 7.7%. The crystals belonged to space group P3121, with unit-cell parameters a = b = 59.50, c = 79.06 Å.
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This is the publisher's version, also available electronically from "http://scripts.iucr.org".
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Citation
Zhao, H., Heroux, A., Sequeira, R., & Tang, L. (2009). Preliminary crystallographic studies of the regulatory domain of response regulator YycF from an essential two-component signal transduction system. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 65(7), 719-722. http://www.dx.doi.org/10.1107/S1744309109022696
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