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MINIREVIEW

Conformational Changes of Spo0F along the Phosphotransfer Pathway

Division of Cellular Biology, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, California 92037

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.

This article has been cited by other articles:

• Varughese, K. I., Tsigelny, I., Zhao, H. (2006). The Crystal Structure of Beryllofluoride Spo0F in Complex with the Phosphotransferase Spo0B Represents a Phosphotransfer Pretransition State. J. Bacteriol. 188: 4970-4977 [Abstract] [Full Text]  
• Wemmer, D. E., Kern, D. (2005). Rebuttal: Conformational Changes of Spo0F along the Phosphotransfer Pathway. J. Bacteriol. 187: 8228-8228 [Full Text]  
• Varughese, K. I. (2005). Rebuttal: Beryllofluoride Binding Mimics Phosphorylation of Aspartate in Response Regulators. J. Bacteriol. 187: 8231-8231 [Full Text]