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Title: Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni

Abstract

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.

Authors:
 [1];  [2]; ;  [3];  [4];  [1];  [5];  [2];  [5]
  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)
  5. (United States)
Publication Date:
OSTI Identifier:
22360250
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 1; Other Information: PMCID: PMC2330109; PMID: 17183170; PUBLISHER-ID: gj5010; OAI: oai:pubmedcentral.nih.gov:2330109; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; DNA; LIGANDS; PROTEINS; RESOLUTION; SALTS; SPACE GROUPS; STRUCTURAL MODELS; X-RAY DIFFRACTION

Citation Formats

Su, Chih-Chia, Shi, Feng, Gu, Ruoyu, Li, Ming, McDermott, Gerry, Yu, Edward W., E-mail: ewyu@iastate.edu, Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, Zhang, Qijing, and Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011. Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309106053127.
Su, Chih-Chia, Shi, Feng, Gu, Ruoyu, Li, Ming, McDermott, Gerry, Yu, Edward W., E-mail: ewyu@iastate.edu, Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, Zhang, Qijing, & Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011. Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni. United Kingdom. doi:10.1107/S1744309106053127.
Su, Chih-Chia, Shi, Feng, Gu, Ruoyu, Li, Ming, McDermott, Gerry, Yu, Edward W., E-mail: ewyu@iastate.edu, Department of Physics and Astronomy, Iowa State University, Ames, IA 50011, Zhang, Qijing, and Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011. Mon . "Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni". United Kingdom. doi:10.1107/S1744309106053127.
@article{osti_22360250,
title = {Preliminary structural studies of the transcriptional regulator CmeR from Campylobacter jejuni},
author = {Su, Chih-Chia and Shi, Feng and Gu, Ruoyu and Li, Ming and McDermott, Gerry and Yu, Edward W., E-mail: ewyu@iastate.edu and Department of Physics and Astronomy, Iowa State University, Ames, IA 50011 and Zhang, Qijing and Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011},
abstractNote = {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.},
doi = {10.1107/S1744309106053127},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 63,
place = {United Kingdom},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}