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Phosphate binding in the active centre of tomato multifunctional nuclease TBN1 and analysis of superhelix formation by the enzyme
J. Stránský, T. Koval', T. Podzimek, A. Týcová, P. Lipovová, J. Matoušek, P. Kolenko, K. Fejfarová, J. Dušková, T. Skálová, J. Hašek, J. Dohnálek,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 2014 to 2 years ago
PubMed Central
from 2014 to 1 year ago
Europe PubMed Central
from 2014 to 2 years ago
- MeSH
- Endodeoxyribonucleases chemistry genetics metabolism MeSH
- Phosphates metabolism MeSH
- Crystallization MeSH
- Molecular Sequence Data MeSH
- Multienzyme Complexes chemistry genetics metabolism MeSH
- Plant Proteins chemistry genetics metabolism MeSH
- Protein Structure, Secondary MeSH
- Amino Acid Sequence MeSH
- Solanum lycopersicum enzymology genetics MeSH
- Binding Sites physiology MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
Institute of Biotechnology CAS v v i Vídeňská 1083 142 20 Praha 4 Czech Republic
University of Chemistry and Technology Technická 5 166 28 Praha 6 Czech Republic
References provided by Crossref.org
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