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Structural and functional studies of the response regulator HupR.

Karen M Davies¹, Vasiliki Skamnaki, Louise N Johnson

¹Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.

Journal of Molecular Biology

|April 25, 2006

Summary

HupR, a key regulator in Rhodobacter capsulatus, controls hydrogenase synthesis. Its V-shaped dimeric structure, determined via electron microscopy, reveals domain interactions crucial for its function.

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Area of Science:

Microbiology
Structural Biology
Biochemistry

Background:

HupR is a response regulator controlling [NiFe]hydrogenase synthesis in Rhodobacter capsulatus.
It is part of a two-component system and belongs to the NtrC subfamily of response regulators.

Purpose of the Study:

To determine the 3D structure of the full-length HupR protein in its unphosphorylated state.
To elucidate the structural organization and domain interactions of HupR.

Main Methods:

Two-dimensional crystallization of HupR using the lipid monolayer technique.
3D structure calculation from tilted electron microscope images of negatively stained HupR.
Fitting of known domain structures into the calculated 3D model.

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Main Results:

HupR crystallizes as a dimer forming an elongated, V-shaped structure (80 x 40 x 85 Å).
The monomer comprises N-terminal receiver, central, and C-terminal DNA-binding domains.
Dimer contact is proposed to occur through the central domain; the N-terminal domain interacts with the lipid monolayer.
The isolated central domain forms a pentamer and lacks ATPase activity.

Conclusions:

The study provides the first 3D structural model of HupR, revealing its dimeric organization and domain arrangement.
Structural insights suggest a mechanism for HupR dimerization and interaction with regulatory components.
The distinct behavior of the isolated central domain highlights its specific role within the HupR structure.