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| {{STRUCTURE_1zn2| PDB=1zn2 | SCENE= }} | | {{STRUCTURE_1zn2| PDB=1zn2 | SCENE= }} |
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| '''Low Resolution Structure of Response Regulator StyR'''
| | ===Low Resolution Structure of Response Regulator StyR=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16154086}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16154086 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16154086}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Styrene degradation]] | | [[Category: Styrene degradation]] |
| [[Category: Transcription regulation]] | | [[Category: Transcription regulation]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:49:58 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 09:19:30 2008'' |
