The 716-amino-acid guanidino kinase from the parasitic flatworm Schistosoma mansoni results from the fusion of two guanidino kinase subunits. Crystals of this 80 kDa protein have been obtained in the monoclinic space group P2 1 , with unit-cell parameters a = 52.7, b = 122.1, c = 63.2 Å , = 108.5 . Synchrotron data were collected to 2.8 Å resolution on ESRF beamline ID29. The structure was solved by the molecular-replacement method, using the 357-amino-acid structure of the arginine kinase from Trypanosoma cruzi as the search model.
Background: Trematode taurocyamine kinases are contiguous dimers of unknown structure. Results: The first reported crystal structure of taurocyamine kinase displays an original bilobal arrangement compared with true dimeric phosphagen kinases. Conclusion: Each lobe is capable of enzymatic activity and substrate binding in a non-mutually exclusive manner. Significance: This structure can serve as a tool for the rational design of anti-schistosomiasis drugs.
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