1yio
From Proteopedia
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| - | [[Image:1yio.gif|left|200px]] | + | [[Image:1yio.gif|left|200px]] |
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| - | '''Crystallographic structure of response regulator StyR from Pseudomonas fluorescens''' | + | {{Structure |
| + | |PDB= 1yio |SIZE=350|CAPTION= <scene name='initialview01'>1yio</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene> and <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystallographic structure of response regulator StyR from Pseudomonas fluorescens''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YIO is a [ | + | 1YIO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YIO OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16154086 16154086] |
[[Category: Pseudomonas fluorescens]] | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:23:21 2008'' |
Revision as of 13:23, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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