1yio
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(New page: 200px<br /><applet load="1yio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yio, resolution 2.20Å" /> '''Crystallographic str...)
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Revision as of 02:02, 25 November 2007
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Crystallographic structure of response regulator StyR from Pseudomonas fluorescens
Overview
StyR belongs to the FixJ subfamily of signal transduction response, regulators; it controls transcription of the styABCD operon coding for, styrene catabolism in Pseudomonas fluorescens ST. The crystal structure of, unphosphorylated StyR is reported at 2.2 A resolution. StyR is composed of, an N-terminal regulatory domain (StyR-N) and a C-terminal DNA binding, domain (StyR-C). The two domains are separated by an elongated linker, alpha helix (34 residues), a new feature in known response regulator, structures. StyR-C is structured similarly to the DNA binding domain of, the response regulator NarL. StyR-N shows structural reorganization of the, phosphate receiving region involved in activation/homodimerization:, specific residues adopt an "active-like" conformation, and the alpha4, helix, involved in dimerization of the homologous FixJ response regulator, is trimmed to just one helical turn. Overall, structural considerations, suggest that phosphorylation may act as an allosteric switch, shifting a, preexisting StyR equilibrium toward the active, dimeric, DNA binding form.
About this Structure
1YIO is a Single protein structure of sequence from Pseudomonas fluorescens with HG and MG as ligands. Full crystallographic information is available from OCA.
Reference
An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation- dependent allosteric activation mechanism., Milani M, Leoni L, Rampioni G, Zennaro E, Ascenzi P, Bolognesi M, Structure. 2005 Sep;13(9):1289-97. PMID:16154086
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