Campus Units

Biochemistry, Biophysics and Molecular Biology, Physics and Astronomy, Veterinary Microbiology and Preventive Medicine

Document Type

Article

Publication Version

Published Version

Publication Date

2007

Journal or Book Title

Acta Crystallographica Section F

Volume

63

Issue

1

First Page

34

Last Page

36

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.

Comments

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

Copyright Owner

International Union of Crystallography

Language

en

File Format

application/pdf