Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni

Journal Article · Mon Jan 01 04:00:00 EST 2007 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106053127· OSTI ID:22360250

Su, Chih-Chia ^[1]; Shi, Feng ^[2]; Gu, Ruoyu; Li, Ming ^[3]; McDermott, Gerry ^[4]; Zhang, Qijing ^[2]

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1. Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011 (United States)
2. Department of Veterinary Microbiology, College of Veterinary Medicine, Iowa State University, Ames, IA 50011 (United States)
3. Department of Physics and Astronomy, Iowa State University, Ames, IA 50011 (United States)
4. Department of Anatomy, School of Medicine, University of California, San Francisco, CA 94143 (United States)

The transcriptional regulator CmeR from C. jejuni has been purified and crystallized and X-ray diffraction data have been collected to a resolution of 2.2 Å. 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 P2{sub 1}2{sub 1}2, 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.

• OSTI ID: 22360250
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALS
DNA
LIGANDS
PROTEINS
RESOLUTION
SALTS
SPACE GROUPS
STRUCTURAL MODELS
X-RAY DIFFRACTION