1ZN2: Low Resolution Structure Of Response Regulator Styr

Citation:
Abstract
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.
PDB ID: 1ZN2Download
MMDB ID: 35125
PDB Deposition Date: 2005/5/11
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.91  Å
Source Organism:
Similar Structures:
Biological Unit for 1ZN2: monomeric; determined by author
Molecular Components in 1ZN2
Label Count Molecule
Protein (1 molecule)
1
Response Regulatory Protein
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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