Article
Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni
Acta Crystallographica Section F
Document Type
Article
Disciplines
Publication Version
Published Version
Publication Date
1-1-2007
DOI
10.1107/S1744309106053127
Abstract
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.
Copyright Owner
International Union of Crystallography
Copyright Date
2007
Language
en
File Format
application/pdf
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: http://works.bepress.com/qijing-zhang/14/
This article is from Acta Crystallographica Section F 63 (2007): 34, doi:10.1107/S1744309106053127. Posted with permission.