PMID:17950313: Difference between revisions
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!align=left |Citation | |||
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'''Li, M, Gu, R, Su, CC, Routh, MD, Harris, KC, Jewell, ES, McDermott, G and Yu, EW''' (2007) Crystal structure of the transcriptional regulator AcrR from Escherichia coli.''J. Mol. Biol.'' '''374''':591-603 | |||
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!align=left |Abstract | |||
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The AcrAB multidrug efflux pump, which belongs to the resistance nodulation division (RND) family, recognizes and extrudes a wide range of antibiotics and chemotherapeutic agents and causes the intrinsic antibiotic resistance in Escherichia coli. The expression of AcrAB is controlled by the transcriptional regulator AcrR, whose open reading frame is located 141 bp upstream of the acrAB operon. To understand the structural basis of AcrR regulation, we have determined the crystal structure of AcrR to 2.55-A resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Each monomer of AcrR forms a multientrance pocket of 350 A(3) in the ligand-binding domain. The ligand-binding pocket is surrounded with mostly hydrophobic residues. In addition, a completely buried negatively charged glutamate, expected to be critical for drug binding, is located at the center of the binding pocket. The crystal structure provides novel insight into the mechanisms of ligand binding and AcrR regulation. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=17950313 PubMed] | |||
Online version:[http://dx.doi.org/10.1016/j.jmb.2007.09.064 10.1016/j.jmb.2007.09.064] | |||
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!align=left |Keywords | |||
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Base Sequence; Binding Sites; Chromatography, Gel; Crystallography, X-Ray; DNA Primers; DNA, Bacterial; Escherichia coli Proteins; Fluorescence Polarization; Ligands; Models, Molecular; Protein Conformation; Repressor Proteins; Transcription Factors | |||
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==Significance {{HelpIcon|Help:Literature}} == | |||
{{LitSignificance}} | |||
== Useful Materials and Methods {{HelpIcon|Help:Literature}}== | |||
{{LitMaterials}} | |||
==Annotations {{HelpIcon|Help:Literature}}== | |||
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!|Gene product!!Qualifier!!GO ID!!GO term name!!Evidence Code!!with/from!!Aspect!!Notes!!Status | |||
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==EcoliWiki Links {{HelpIcon|Help:Literature}} == | |||
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==See also== | |||
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Revision as of 10:44, 19 April 2012
| Citation |
Li, M, Gu, R, Su, CC, Routh, MD, Harris, KC, Jewell, ES, McDermott, G and Yu, EW (2007) Crystal structure of the transcriptional regulator AcrR from Escherichia coli.J. Mol. Biol. 374:591-603 |
|---|---|
| Abstract |
The AcrAB multidrug efflux pump, which belongs to the resistance nodulation division (RND) family, recognizes and extrudes a wide range of antibiotics and chemotherapeutic agents and causes the intrinsic antibiotic resistance in Escherichia coli. The expression of AcrAB is controlled by the transcriptional regulator AcrR, whose open reading frame is located 141 bp upstream of the acrAB operon. To understand the structural basis of AcrR regulation, we have determined the crystal structure of AcrR to 2.55-A resolution, revealing a dimeric two-domain molecule with an entirely helical architecture similar to members of the TetR family of transcriptional regulators. Each monomer of AcrR forms a multientrance pocket of 350 A(3) in the ligand-binding domain. The ligand-binding pocket is surrounded with mostly hydrophobic residues. In addition, a completely buried negatively charged glutamate, expected to be critical for drug binding, is located at the center of the binding pocket. The crystal structure provides novel insight into the mechanisms of ligand binding and AcrR regulation. |
| Links |
PubMed Online version:10.1016/j.jmb.2007.09.064 |
| Keywords |
Base Sequence; Binding Sites; Chromatography, Gel; Crystallography, X-Ray; DNA Primers; DNA, Bacterial; Escherichia coli Proteins; Fluorescence Polarization; Ligands; Models, Molecular; Protein Conformation; Repressor Proteins; Transcription Factors |
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| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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