Molecular recognition of bacterial phosphorelay proteins.
The transfer of the phosphoryl group from a histidine kinase to a response regulator forms the basis of bacterial signal transduction. The critical question of how a component of a signal transduction system specifically associates with its partner to produce the ideal environment for phosphotransfer is addressed in this review in the light of the structure of the Spo0F-Spo0B complex in Bacillus subtilis.
Varughese
Kottayil Iype
KI
Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA. kiv@scripps.edu
D001412:Bacillus subtilis / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010744:Phosphoric Monoester Hydrolases / Q000737:chemistry* / Q000378:metabolism; D010770:Phosphotransferases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D020218:Response Elements; D012808:Sigma Factor; D015398:Signal Transduction; D014157:Transcription Factors
D001426:Bacterial Proteins; D012808:Sigma Factor; C080951:Spo0F protein, Bacillus subtilis; D014157:Transcription Factors; C092468:spoIIR protein, Bacillus subtilis; C030069:spore-specific proteins, Bacillus; D010770:Phosphotransferases; D010744:Phosphoric Monoester Hydrolases