Skip to main content
Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni
Acta Crystallographica Section F
  • Chih-chia Su, Iowa State University
  • Feng Shi, Iowa State University
  • Ruoyu Gu, Iowa State University
  • Ming Li, Iowa State University
  • Gerry McDermott, University of California - Berkeley
  • Edward Yu, Iowa State University
  • Qijing Zhang, Iowa State University
Document Type
Publication Version
Published Version
Publication Date
In Campylobacter jejuni, a Gram-negative bacterial pathogen causing gastroenteritis in humans, the CmeR regulatory protein controls transcription of the multidrug transporter gene operon cmeABC. CmeR belongs to the TetR family of transcriptional regulators. The 210-residue CmeR consists of two functional motifs: an N-terminal DNA-binding domain and a C-terminal ligand-binding domain. It is predicted that the DNA-binding domain interacts directly with target promoters, while the C-terminal motif interacts with inducing ligands (such as bile salts). As an initial step towards confirming this structural model, recombinant CmeR protein containing a 6×His tag at the N-terminus was crystallized. Crystals of ligand-free CmeR belonged to space group P21212, with unit-cell parameters a = 37.4, b = 57.6, c = 93.3 Å. Diffraction was observed to at least 2.2 Å at 100 K. Analysis of the detailed CmeR structure is currently in progress.

This article is from Acta Crystallographica Section F 63 (2007): 34, doi:10.1107/S1744309106053127. Posted with permission.

Copyright Owner
International Union of Crystallography
File Format
Citation Information
Chih-chia Su, Feng Shi, Ruoyu Gu, Ming Li, et al.. "Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni" Acta Crystallographica Section F Vol. 63 Iss. 1 (2007) p. 34 - 36
Available at: