This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bachhawat, P.
Right arrow Articles by Stock, A. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bachhawat, P.
Right arrow Articles by Stock, A. M.

 Previous Article  |  Next Article 

Journal of Bacteriology, August 2007, p. 5987-5995, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00049-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Crystal Structures of the Receiver Domain of the Response Regulator PhoP from Escherichia coli in the Absence and Presence of the Phosphoryl Analog Beryllofluoride{triangledown}

Priti Bachhawat1 and Ann M. Stock1,2*

Center for Advanced Biotechnology and Medicine, Department of Biochemistry,1 Howard Hughes Medical Institute, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 088542

Received 10 January 2007/ Accepted 23 May 2007

The response regulator PhoP is part of the PhoQ/PhoP two-component system involved in responses to depletion of extracellular Mg2+. Here, we report the crystal structures of the receiver domain of Escherichia coli PhoP determined in the absence and presence of the phosphoryl analog beryllofluoride. In the presence of beryllofluoride, the active receiver domain forms a twofold symmetric dimer similar to that seen in structures of other regulatory domains from the OmpR/PhoB family, providing further evidence that members of this family utilize a common mode of dimerization in the active state. In the absence of activating agents, the PhoP receiver domain crystallizes with a similar structure, consistent with the previous observation that high concentrations can promote an active state of PhoP independent of phosphorylation.

* Corresponding author. Mailing address: CABM, 679 Hoes Lane, Piscataway, NJ 08854-5627. Phone: (732) 235-4844. Fax: (732) 235-5289. E-mail: stock{at}cabm.rutgers.edu

{triangledown} Published ahead of print on 1 June 2007.

Journal of Bacteriology, August 2007, p. 5987-5995, Vol. 189, No. 16
0021-9193/07/$08.00+0     doi:10.1128/JB.00049-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Perez, J. C., Groisman, E. A. (2009). Transcription factor function and promoter architecture govern the evolution of bacterial regulons. Proc. Natl. Acad. Sci. USA 106: 4319-4324 [Abstract] [Full Text]  
  • Weigt, M., White, R. A., Szurmant, H., Hoch, J. A., Hwa, T. (2009). Identification of direct residue contacts in protein-protein interaction by message passing. Proc. Natl. Acad. Sci. USA 106: 67-72 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»