A Metal–Ligand-mediated Intersubunit Allosteric Switch in Related SmtB/ArsR Zinc Sensor Proteins

The origin of metal ion selectivity by members of the SmtB/ArsR family of bacterial metal-sensing transcriptional repressors and the mechanism of negative allosteric regulation of DNA binding is poorly understood. Here, we report that two homologous zinc sensors, Staphylococcus aureus CzrA and cyano...

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Veröffentlicht in:	Journal of molecular biology 2003-10, Vol.333 (4), p.683-695
Hauptverfasser:	Eicken, Christoph, Pennella, Mario A., Chen, Xiaohua, Koshlap, Karl M., VanZile, Michael L., Sacchettini, James C., Giedroc, David P.
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation allostery Amino Acid Sequence ArsR protein Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Crystallography, X-Ray Cyanobacteria - metabolism Dimerization DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism histidine Hydrogen Bonding Ligands metal sensing Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Quaternary Protein Subunits - chemistry Protein Subunits - metabolism Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism Sequence Alignment SmtB protein Staphylococcus aureus Staphylococcus aureus - metabolism Trans-Activators - chemistry Trans-Activators - metabolism transcriptional regulation x-ray structure zinc Zinc - chemistry
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