1yio
From Proteopedia
(New page: 200px<br /><applet load="1yio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yio, resolution 2.20Å" /> '''Crystallographic str...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1yio.gif|left|200px]]<br /><applet load="1yio" size=" | + | [[Image:1yio.gif|left|200px]]<br /><applet load="1yio" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yio, resolution 2.20Å" /> | caption="1yio, resolution 2.20Å" /> | ||
'''Crystallographic structure of response regulator StyR from Pseudomonas fluorescens'''<br /> | '''Crystallographic structure of response regulator StyR from Pseudomonas fluorescens'''<br /> | ||
==Overview== | ==Overview== | ||
| - | StyR belongs to the FixJ subfamily of signal transduction response | + | 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== | ==About this Structure== | ||
| - | 1YIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with HG and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens] with <scene name='pdbligand=HG:'>HG</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIO OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:05:43 2008'' |
Revision as of 14:05, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 16:05:43 2008
