4LRZ: Crystal Structure of the E.coli DhaR(N)-DhaL complex

Escherichia coli dihydroxyacetone (Dha) kinase consists of two subunits, DhaK and DhaL. Transcription of dha operon is regulated by the DhaR transcription factor and its action is under control of the kinase subunits. DhaR is activated by interaction with DhaL while it is repressed by DhaK. We have determined the structures of DhaK and DhaL bound to the tandem GAF-like and PAS domains of the DhaR, providing an architectural model for how GAF/PAS tandem domains work together in binding protein partners. The structures reveal a mechanism of opposite transcriptional regulation by the DhaK and DhaL subunits. The kinase subunits interface with DhaR through surfaces that partially overlap with their active sites, allowing sensing of ATP- versus ADP-loaded DhaL subunit and also precluding a ternary complex between DhaK-DhaL and DhaR. The rotation of helices within the DhaR coiled-coil linker upon DhaL binding provides the mechanism for transmitting the binding signal from the GAF/PAS domains to the C-terminal DNA-binding domain.
PDB ID: 4LRZDownload
MMDB ID: 117058
PDB Deposition Date: 2013/7/21
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.32  Å
Source Organism:
Similar Structures:
Biological Unit for 4LRZ: tetrameric; determined by author and by software (PISA)
Molecular Components in 4LRZ
Label Count Molecule
Proteins (4 molecules)
Pts-dependent Dihydroxyacetone Kinase, Adp-binding Subunit Dhal(Gene symbol: dhaL)
Molecule annotation
Pts-dependent Dihydroxyacetone Kinase Operon Regulatory Protein(Gene symbol: dhaR)
Molecule annotation
Chemicals (6 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB