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Resonance assignments of the metal sensor CzrA in the apo-, Zn2- and DNA-bound (42 kDa) states

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Abstract

Zn/Co binding to homodimeric CzrA de-represses transcription of the czr (cobalt zinc resistance) operon in Staphylococcus aureus. Essentially complete backbone and stereospecific methyl group resonance assignments for apo-, Zn2 and a 42 kDa apo–CzrA–DNA complex are presented.

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Acknowledgements

This work was supported by grants from the NIH (GM042569 to D.P.G.) and the Robert A. Welch Foundation (A-1295). The NMR spectrometers at Texas A&M University were obtained in part from support from the NSF. M.A.P. was supported in part by a NIH Chemistry-Biology Interface Training Program (T32 GM008523). M.A.P. present address: Department of Microbiology, Immunology and Molecular Genetics, Molecular Biology Institute, University of California, Los Angeles, CA 90095–1570, USA.

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Correspondence to David P. Giedroc.

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Arunkumar, A.I., Pennella, M.A., Kong, X. et al. Resonance assignments of the metal sensor CzrA in the apo-, Zn2- and DNA-bound (42 kDa) states. Biomol NMR Assign 1, 99–101 (2007). https://doi.org/10.1007/s12104-007-9027-y

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  • DOI: https://doi.org/10.1007/s12104-007-9027-y

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