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Prague, Czech Republic

Stransky J.,Institute Of Biotechnology Cas Vvi | Stransky J.,Czech Technical University | Koval' T.,Institute Of Biotechnology Cas Vvi | Koval' T.,Czech Institute of Macromolecular Chemical | And 15 more authors.
Acta Crystallographica Section:F Structural Biology Communications | Year: 2015

Tomato multifunctional nuclease TBN1 belongs to the type I nuclease family, which plays an important role in apoptotic processes and cell senescence in plants. The newly solved structure of the N211D mutant is reported. Although the main crystal-packing motif (the formation of superhelices) is conserved, the details differ among the known structures. A phosphate ion was localized in the active site of the enzyme. The binding of the surface loop to the active centre is stabilized by the phosphate ion, which correlates with the observed aggregation of TBN1 in phosphate buffer. The conserved binding of the surface loop to the active centre suggests biological relevance of the contact in a regulatory function or in the formation of oligomers. © 2015 International Union of Crystallography.

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