Conformational changes of Spo0F along the phosphotransfer pathway.
Spo0F is a secondary messenger in the sporulation phosphorelay, and its structure has been characterized crystallographically in the apo-state, in the metal-bound state, and in an interacting state with a phosphotransferase. Additionally, the solution structure of the molecule has been characterized by nuclear magnetic resonance techniques in the unliganded state and in complex with beryllofluoride. Spo0F is a single-domain protein with a well-defined three-dimensional structure, but it is capable of adapting to specific conformations for catching and releasing the phosphoryl moiety. This commentary deals with the conformational fluctuations of the molecule as it moves from an apo-state to a metal-coordinated state, to a phosphorylated state, and then to a phosphoryl-transferring state.
Varughese
Kottayil I
KI
Division of Cellular Biology, Department of Molecular and Experimental Medicine, MEM-116, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. kiv@scripps.edu
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001608:Beryllium / Q000378:metabolism; D001665:Binding Sites; D018360:Crystallography, X-Ray; D005459:Fluorides / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D010766:Phosphorylation; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D015290:Second Messenger Systems; D013816:Thermodynamics
D001426:Bacterial Proteins; C080951:Spo0F protein, Bacillus subtilis; C035982:beryllium fluoride; D001608:Beryllium; D005459:Fluorides