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Título: | Tandem DNA Recognition by PhoB, a two-component signal transduction transcriptional activator |
Autor: | Blanco, Alexandre G.; Solà, Maria CSIC ORCID ; Gomis-Rüth, F. Xavier CSIC ORCID ; Coll, Miquel CSIC ORCID | Palabras clave: | DNA binding domains PhoB Tandem protein-DNA complex Two-component signal transduction Crystal structures |
Fecha de publicación: | 2002 | Editor: | Cell Press | Citación: | Structure 10(5): 701-713 (2002) | Resumen: | PhoB is a signal transduction response regulator that activates nearly 40 genes in phosphate depletion conditions in E. coli and closely related bacteria. The structure of the PhoB effector domain in complex with its target DNA sequence, or pho box, reveals a novel tandem arrangement in which several monomers bind head to tail to successive 11-base pair direct-repeat sequences, coating one face of a smoothly bent double helix. The protein has a winged helix fold in which the DNA recognition elements comprise helix α3, penetrating the major groove, and a β hairpin wing interacting with a compressed minor groove via Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation loops protrude laterally in an appropriate orientation to interact with the RNA polymerase σ70 subunit, which triggers transcription initiation. | Versión del editor: | http://dx.doi.org/10.1016/S0969-2126(02)00761-X | URI: | http://hdl.handle.net/10261/107599 | DOI: | 10.1016/S0969-2126(02)00761-X | Identificadores: | doi: 10.1016/S0969-2126(02)00761-X issn: 0969-2126 |
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