Crystal structure of a phosphatase-resistant mutant of sporulation response regulator Spo0F from Bacillus subtilis.
Madhusudan, Zapf, J., Whiteley, J.M., Hoch, J.A., Xuong, N.H., Varughese, K.I.(1996) Structure 4: 679-690
- PubMed: 8805550 
- DOI: https://doi.org/10.1016/s0969-2126(96)00074-3
- Primary Citation of Related Structures:  
1SRR - PubMed Abstract: 
Spo0F, a phosphotransferase containing an aspartyl pocket, is involved in the signaling pathway (phosphorelay) controlling sporulation in Bacillus subtilis. It belongs to the superfamily of bacterial response regulatory proteins, which are activated upon phosphorylation of an invariant aspartate residue. This phosphorylation is carried out in a divalent cation dependent reaction catalyzed by cognate histidine kinases. Knowledge of the Spo0F structure would provide valuable information that would enable the elucidation of its function as a secondary messenger in a system in which a phosphate is donated from Spo0F to Spo0B, the third of four main proteins that constitute the phosphorelay.
Organizational Affiliation: 
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA.