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- W2033291218 abstract "Two-dimensional crystals of the histidine-tagged-HupR protein, a transcriptional regulator from the photosynthetic bacterium Rhodobacter capsulatus, were obtained upon specific interaction with a Ni2+-chelated lipid monolayer. HupR is a response regulator of the NtrC family; it activates the transcription of the structural genes, hupSLC, of the [NiFe]hydrogenase. The lipid (Ni-NTA-DOGA) uses the metal chelator nitrilotriacetic group as the hydrophilic headgroup and contains unsaturated oleyl tails to provide the fluidity necessary for two-dimensional protein crystallization. A projection map of the full-length protein at 18 Å resolution was generated by analysing electron microscopy micrographs of negatively stained crystals. The HupR protein appeared to be dimeric and revealed a characteristic “propeller-like” motif. Each monomer forms an L-shaped structure." @default.
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- W2033291218 date "1997-12-01" @default.
- W2033291218 modified "2023-10-18" @default.
- W2033291218 title "Structural study of the response regulator HupR from Rhodobacter capsulatus. electron microscopy of two-dimensional crystals on a nickel-chelating lipid" @default.
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- W2033291218 doi "https://doi.org/10.1006/jmbi.1997.1431" @default.
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