Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme

0454706 - ÚMCH 2016 RIV GB eng J - Journal Article
Stránský, J. - Koval, Tomáš - Podzimek, T. - Týcová, A. - Lipovová, P. - Matoušek, J. - Kolenko, Petr - Fejfarová, Karla - Dušková, J. - Skálová, T. - Hašek, J. - Dohnálek, Jan
Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme.
Acta Crystallographica Section F-Structural Biology Communications. Roč. 71, č. 11 (2015), s. 1408-1415. E-ISSN 2053-230X
R&D Projects: GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) EE2.3.30.0029
Institutional support: RVO:61389013
Keywords : tomato multifunctional nuclease * TBN1 * type I nuclease
Subject RIV: EB - Genetics ; Molecular Biology
Impact factor: 0.647, 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.
Permanent Link: http://hdl.handle.net/11104/0255966