Article
Dimerization properties of the RpBphP2 chromophore-binding domain crystallized by homologue-directed mutagenesis.
Acta crystallographica. Section D, Biological crystallography - 1 Aug 2012
Bellini Dom, Papiz Miroslav Z
Abstract excerpt
Bacteriophytochromes (BphPs) are biliverdin IXα-containing photoreceptors that photoconvert between red (Pr) and far-red (Pfr) absorbing states. BphPs are one half of a two-component system that transmits a light signal to a histidine kinase domain and then to a gene-response regulator. In Rhodopseudomonas palustris, synthesis of a light-harvesting complex (LH4) is controlled by two BphPs (RpBphP2 and RpBphP3)....
Topics
- Bacterial Proteins
- Chromatography, Gel
- Chromatophores
- Cloning, Molecular
- Crystallization
- Crystallography, X-Ray
- Dimerization
- Light-Harvesting Protein Complexes
- Models, Chemical
- Molecular Conformation