Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni

Date
2007-01-01
Authors
Yu, Edward
Su, Chih-chia
Shi, Feng
Gu, Ruoyu
Zhang, Qijing
Li, Ming
McDermott, Gerry
Yu, Edward
Zhang, Qijing
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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.

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<p>This article is from <em>Acta Crystallographica Section F</em> 63 (2007): 34, <a href="http://dx.doi.org/10.1107/S1744309106053127" target="_blank">doi:10.1107/S1744309106053127</a>. Posted with permission.</p>
Keywords
CmeR, transcriptional regulators, gene regulation, multi-ligand recognition
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